2.0 2012-05-31 10:27:32 -0600 2015-09-13 12:56:08 -0600 ECMDB00574 M2MDB000152 L-Cysteine Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible: as reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. Oxidation of cysteine can produce a disulfide bond with another thiol, or further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead and cadmium tightly.Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is important in energy metabolism. (http://www.dcnutrition.com/AminoAcids/) (+)-2-Amino-3-mercaptopropionate (+)-2-Amino-3-mercaptopropionic acid (2R)-2-amino-3-mercaptopropanoate (2R)-2-amino-3-mercaptopropanoic acid (2R)-2-amino-3-sulfanylpropanoate (2R)-2-amino-3-sulfanylpropanoic acid (2R)-2-amino-3-sulphanylpropanoate (2R)-2-amino-3-sulphanylpropanoic acid (R)-(+)-cysteine (R)-2-amino-3-mercapto-Propanoate (R)-2-amino-3-mercapto-Propanoic acid (R)-2-Amino-3-mercaptopropanoate (R)-2-Amino-3-mercaptopropanoic acid (R)-cysteine 2-Amino-3-mercaptopropanoate 2-Amino-3-mercaptopropanoic acid 2-Amino-3-mercaptopropionate 2-Amino-3-mercaptopropionic acid 3-Mercapto-L-Alanine a-amino-b-Thiolpropionate a-amino-b-Thiolpropionic acid Acetylcysteine Alpha-Amino-beta-thiolpropionate Alpha-Amino-beta-thiolpropionic acid B-Mercaptoalanine Beta-Mercaptoalanine C Carbocysteine Cisteina Cisteinum Cys Cystein Cysteine Cysteinum Free cysteine Half-cystine L Cysteine L-(+)-Cysteine L-2-Amino-3-mercaptopropanoate L-2-Amino-3-mercaptopropanoic acid L-2-Amino-3-mercaptopropionate L-2-Amino-3-mercaptopropionic acid L-Cystein L-Cysteine Polycysteine Thioserine α-amino-β-Thiolpropionate α-amino-β-Thiolpropionic acid β-Mercaptoalanine C3H7NO2S 121.158 121.019749163 (2R)-2-amino-3-sulfanylpropanoic acid L-cysteine 52-90-4 N[C@@H](CS)C(O)=O InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 XUJNEKJLAYXESH-REOHCLBHSA-N Solid Cytosol Extra-organism Periplasm logp -2.57 ALOGPS logs -0.72 ALOGPS solubility 2.31e+01 g/l ALOGPS melting_point 220 oC logp -2.8 ChemAxon pka_strongest_acidic 2.35 ChemAxon pka_strongest_basic 9.05 ChemAxon iupac (2R)-2-amino-3-sulfanylpropanoic acid ChemAxon average_mass 121.158 ChemAxon mono_mass 121.019749163 ChemAxon smiles N[C@@H](CS)C(O)=O ChemAxon formula C3H7NO2S ChemAxon inchi InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 ChemAxon inchikey XUJNEKJLAYXESH-REOHCLBHSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 28.22 ChemAxon polarizability 11.41 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 3 ChemAxon donor_count 3 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Glutathione metabolism The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione. This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. PW000833 ec00480 Metabolic Cysteine and methionine metabolism ec00270 Glycine, serine and threonine metabolism ec00260 Pantothenate and CoA biosynthesis The CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate. The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate. On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine. Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid. Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine. The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA. Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A. . The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III. The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth. The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06]. PW000828 ec00770 Metabolic Selenoamino acid metabolism ec00450 Sulfur metabolism The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000922 ec00920 Metabolic Aminoacyl-tRNA biosynthesis ec00970 Taurine and hypotaurine metabolism ec00430 Thiamine metabolism ec00730 Microbial metabolism in diverse environments ec01120 Sulfur relay system ec04122 Metabolic pathways eco01100 L-alanine metabolism L-alanine is an essential component of proteins and peptidoglycan. The latter also contains about three molecules of D-alanine for every L-alanine. Only about 10 percent of the total alanine synthesized flows into peptidoglycan. There are at least 3 ways to begin the biosynthesis of alanine. The first method for alanine biosynthesis begins with L-cysteine produced from L-cysteine biosynthesis pathway. L-cysteine reacts with an [L-cysteine desulfurase] L-cysteine persulfide through a cysteine desulfurase resulting in a release of [L-cysteine desulfurase] l-cysteine persulfide and L-alanine. The second method starts with pyruvic acid reacting with L-glutamic acid through a glutamate-pyruvate aminotransferase resulting in a oxoglutaric acid and L-alanine. The third method starts with L-glutamic acid interacting with Alpha-ketoisovaleric acid through a valine transaminase resulting in an oxoglutaric acid and L-valine. L-valine reacts with pyruvic acid through a valine-pyruvate aminotransferase resulting Alpha-ketoisovaleric acid and L-alanine. This first step of the pathway, which can be catalyzed by either of two racemases( biosynthetic or catabolic), also serves an essential role in biosynthesis because its product, D-alanine, is an essential component of cell wall peptidoglycan (murein). D-alanine is metabolized by an ATP driven D-alanine ligase A and B resulting in D-alanyl-D-alanine. This product is incorporated into the peptidoglycan biosynthesis. L-alanine is metabolized with alanine racemase, either catabolic or metabolic resulting in a D-alanine. This compound reacts with water and a quinone through a D-amino acid dehydrogenase resulting in Pyruvic acid, hydroquinone and ammonium, thus entering the central metabolism and thereby can serve as a total source of carbon and energy. This pathway is unique among those through which L-amino acids are degraded, in that the L form must first be converted to the D form. D-alanine, is an essential component of cell wall peptidoglycan (murein). The role of the alr racemase is predominately biosynthetic: it is produced constitutively in small amounts. The role of the dadX racemase is degradative: it is induced to high levels by alanine and is subject to catabolite repression. PW000788 Metabolic Secondary Metabolites: cysteine biosynthesis from serine The pathway starts with a 3-phosphoglyceric acid interacting with an NAD driven D-3-phosphoglycerate dehydrogenase / α-ketoglutarate reductase resulting in an NADH, a hydrogen ion and a phosphohydroxypyruvic acid. This compound then interacts with an L-glutamic acid through a 3-phosphoserine aminotransferase / phosphohydroxythreonine aminotransferase resulting in a oxoglutaric acid and a DL-D-phosphoserine. The latter compound then interacts with a water molecule through a phosphoserine phosphatase resulting in a phosphate and an L-serine. The L-serine interacts with an acetyl-coa through a serine acetyltransferase resulting in a release of a Coenzyme A and a O-Acetylserine. The O-acetylserine then interacts with a hydrogen sulfide through a O-acetylserine sulfhydrylase A resulting in an acetic acid, a hydrogen ion and an L-cysteine PW000977 Metabolic cysteine biosynthesis The pathway of cysteine biosynthesis is a two-step conversion starting from L-serine and yielding L-cysteine. L-serine biosynthesis is shown for context. L-cysteine can also be synthesized from sulfate derivatives. The process through L-serine involves a serine acetyltransferase that produces a O-acetylserine which reacts together with hydrogen sulfide through a cysteine synthase complex in order to produce L-cysteine and acetic acid. Hydrogen sulfide is produced from a sulfate. Sulfate reacts with sulfate adenylyltransferase to produce adenosine phosphosulfate. This compound in turn is phosphorylated through a adenylyl-sulfate kinase into a phosphoadenosine phosphosulfate which in turn reacts with a phosphoadenosine phosphosulfate reductase to produce a sulfite. The sulfite reacts with a sulfite reductase to produce the hydrogen sulfide. This pathway is regulated at the genetic level in its second step, wtih both cysteine synthase isozymes being under the positive control of the cysteine-responsive transcription factor CysB. It is also subject to very strong feedback inhibition of its first step by the final pathway product, cysteine. Although two cysteine synthase isozymes exist, only cysteine synthase A (CysK) forms a complex with serine acetyltransferase. CysK is also the only one of the two cysteine synthases that is required for cell viability on cysteine-free medium. Both steps in this pathway are reversible. Based on genetic and proteomic data, it appears that the cysteine synthases may actually act as a sulfur scavenging system during sulfur starvation, stripping sulfur off of L-cysteine, generating any number of variant amino acids in the process. PW000800 Metabolic methionine biosynthesis The de novo biosynthesis of methionine is an energy-costly process involving inputs from several other pathways. The carbon skeleton of methionine is derived from aspartate. The sulfur is derived from cysteine which derives its sulfur from sulfate assimilation. The methyl group is derived from serine via one-carbon metabolism. Methionine is also converted to S-adenosyl-L-methionine, a methyl group donor, by the product of gene metK . The synthesis starts with a product of the lysine biosynthesis pathway, L-aspartate-semialdehyde. This compound is dehydrogenated by a NADPH aspartate kinase / homoserine dehydrogenase resulting in NADP and L-homoserine. Homoserine is activated by O-succinylation in a reaction catalyzed by MetA. The product O-succinyl-L-homoserine combines with cysteine to form cystathionine in a reaction catalyzed by MetB. Lyase cleavage of cystathionine by MetC forms homocysteine. This β-cystathionase activity can also be supplied by MalY as demonstrated in vivo by the ability of constitutive MalY expression to complement metC mutants auxotrophic for methionine . Homocysteine is subsequently methylated by either MetH or MetE to produce methionine. In E. coli MetH can function only in the presence of exogenously supplied vitamin B12 (cobalamin), which represses MetE expression. B12 is likely to be available in the gut. In the absence of exogenously supplied B12, MetE catalyzes this final step of de novo methionine biosynthesis. L-methionine is then transferred into the periplasmic space through a leucine efflux transporter. Under stressful conditions there is further regulation of the pathway enzymes. Under heat-shock conditions growth is slowed due to the thermal instability of MetA. Oxidative stress affects MetE which contains an oxidation-sensitive cysteine residue at position 645 near the active site. Oxidation of methionone itself can also occur although the cell contains methionine sufloxide reductases MsrA and MsrB to combat this. Weak organic acids also generate oxidative stress, with more complex effects. Sulfur limitation depletes homocysteine which serves as a coactivator for MetR activation of MetE expression. Due to the absence of this pathway in mammals, some of the bacterial biosynthetic enzymes are potential drug targets. In addition, although methionine is used as a food additive and a medication, its industrial scale production in microorganisms has not yet been achieved due to the complexity and strong regulation of its biosynthetic pathway. PW000814 Metabolic sulfur metabolism (butanesulfonate) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000923 Metabolic sulfur metabolism (butanesulfonate/phenylacetaldehyde) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW001012 Metabolic sulfur metabolism (ethanesulfonate) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case ethanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Ethanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000925 Metabolic sulfur metabolism (isethionate) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case isethionate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Isethionate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000926 Metabolic sulfur metabolism (methanesulfonate) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case methanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Methanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000927 Metabolic sulfur metabolism (propanesulfonate) The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 3-(N-morpholino)propanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 3-(N-morpholino)propanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000924 Metabolic tRNA Charging 2 This pathway groups together all E. coli tRNA charging reactions. PW000803 Metabolic tRNA charging This pathway groups together all E. coli tRNA charging reactions. PW000799 Metabolic glutathione metabolism II The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione. This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. Glutathione can then be degraded into various different glutathione containg compounds by reacting with a napthalene through a glutathione S-transferase PW001927 Metabolic glutathione metabolism III The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione. This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. PW002018 Metabolic Hydrogen Sulfide Biosynthesis I It has long been known that many bacteria are able to produce hydrogen sulfide [Barrett87]. However, the physiological role of H2S in nonsulfur bacteria was unknown. A recent report has now shown that production of H2S serves to defend cells from antibiotics by mitigating oxidative stress. This pathway is one of two pathways for hydrogen sulfide biosynthesis. Neither of the two activities have been shown biochemically for the E. coli enzymes. The function of AspC as a cysteine transaminase is hypothesized based on sequence similarity to mammalian enzymes. The function of SseA was determined based on the phenotype of an sseA null mutant, which does not produce hydrogen sulfide. PW002066 Metabolic L-cysteine degradation The degradation of cysteine starts with L-cysteine reacting with l-cysteine desulfhydrase resulting in the release of a hydrogen sulfide, a hydrogen ion and a a 2-aminoprop-2-enoate. The latter compound in turn reacts spontaneously to form a 2-iminopropanoate. This compound in turn reacts spontaneously with water and a hydrogen ion resulting in the release of ammonium and pyruvate. PW002110 Metabolic cysteine biosynthesis I CYSTSYN-PWY thiazole biosynthesis I (E. coli) PWY-6892 molybdenum cofactor biosynthesis PWY-6823 tRNA charging TRNA-CHARGING-PWY methionine biosynthesis I HOMOSER-METSYN-PWY L-cysteine degradation II LCYSDEG-PWY coenzyme A biosynthesis COA-PWY glutathione biosynthesis GLUTATHIONESYN-PWY hydrogen sulfide biosynthesis PWY0-1534 alanine biosynthesis III PWY0-1021 Specdb::CMs 572 Specdb::CMs 573 Specdb::CMs 574 Specdb::CMs 575 Specdb::CMs 576 Specdb::CMs 3282 Specdb::CMs 30101 Specdb::CMs 30201 Specdb::CMs 30306 Specdb::CMs 30307 Specdb::CMs 30592 Specdb::CMs 30734 Specdb::CMs 30756 Specdb::CMs 31774 Specdb::CMs 37632 Specdb::CMs 146278 Specdb::CMs 1066885 Specdb::CMs 1066887 Specdb::CMs 1066889 Specdb::CMs 1066890 Specdb::CMs 1066892 Specdb::NmrOneD 1241 Specdb::NmrOneD 1426 Specdb::NmrOneD 4743 Specdb::NmrOneD 144450 Specdb::NmrOneD 144451 Specdb::NmrOneD 144452 Specdb::NmrOneD 144453 Specdb::NmrOneD 144454 Specdb::NmrOneD 144455 Specdb::NmrOneD 144456 Specdb::NmrOneD 144457 Specdb::NmrOneD 144458 Specdb::NmrOneD 144459 Specdb::NmrOneD 144460 Specdb::NmrOneD 144461 Specdb::NmrOneD 144462 Specdb::NmrOneD 144463 Specdb::NmrOneD 144464 Specdb::NmrOneD 144465 Specdb::NmrOneD 144466 Specdb::NmrOneD 144467 Specdb::NmrOneD 144468 Specdb::NmrOneD 144469 Specdb::NmrOneD 166443 Specdb::MsMs 800 Specdb::MsMs 801 Specdb::MsMs 802 Specdb::MsMs 4204 Specdb::MsMs 4205 Specdb::MsMs 4206 Specdb::MsMs 4207 Specdb::MsMs 4208 Specdb::MsMs 4209 Specdb::MsMs 4210 Specdb::MsMs 4211 Specdb::MsMs 4217 Specdb::MsMs 179826 Specdb::MsMs 179827 Specdb::MsMs 179828 Specdb::MsMs 182160 Specdb::MsMs 182161 Specdb::MsMs 182162 Specdb::MsMs 447649 Specdb::MsMs 447738 Specdb::MsMs 1471148 Specdb::MsMs 2226479 Specdb::MsMs 2228252 Specdb::MsMs 2228881 Specdb::MsMs 2230541 Specdb::NmrTwoD 1024 Specdb::NmrTwoD 1371 HMDB00574 5862 5653 C00097 17561 CYS FCY L-Cysteine Keseler, I. 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Agricultural and Biological Chemistry (1977), 41(10), 2071-5. http://hmdb.ca/system/metabolites/msds/000/000/493/original/HMDB00574.pdf?1358894667 Aspartate aminotransferase P00509 AAT_ECOLI aspC http://ecmdb.ca/proteins/P00509.xml Cystathionine gamma-synthase P00935 METB_ECOLI metB http://ecmdb.ca/proteins/P00935.xml Aminopeptidase N P04825 AMPN_ECOLI pepN http://ecmdb.ca/proteins/P04825.xml Cystathionine beta-lyase metC P06721 METC_ECOLI metC http://ecmdb.ca/proteins/P06721.xml Cysteine desulfurase P0A6B7 ISCS_ECOLI iscS http://ecmdb.ca/proteins/P0A6B7.xml Glutamate--cysteine ligase P0A6W9 GSH1_ECOLI gshA http://ecmdb.ca/proteins/P0A6W9.xml Tryptophanase P0A853 TNAA_ECOLI tnaA http://ecmdb.ca/proteins/P0A853.xml Cysteine synthase A P0ABK5 CYSK_ECOLI cysK http://ecmdb.ca/proteins/P0ABK5.xml Coenzyme A biosynthesis bifunctional protein coaBC P0ABQ0 COABC_ECOLI coaBC http://ecmdb.ca/proteins/P0ABQ0.xml Aminoacyl-histidine dipeptidase P15288 PEPD_ECOLI pepD http://ecmdb.ca/proteins/P15288.xml Cysteine synthase B P16703 CYSM_ECOLI cysM http://ecmdb.ca/proteins/P16703.xml Cysteinyl-tRNA synthetase P21888 SYC_ECOLI cysS http://ecmdb.ca/proteins/P21888.xml Protein malY P23256 MALY_ECOLI malY http://ecmdb.ca/proteins/P23256.xml Peptidase B P37095 PEPB_ECOLI pepB http://ecmdb.ca/proteins/P37095.xml Cytosol aminopeptidase P68767 AMPA_ECOLI pepA http://ecmdb.ca/proteins/P68767.xml Cysteine desulfurase_ P77444 SUFS_ECOLI sufS http://ecmdb.ca/proteins/P77444.xml ATP-binding/permease protein cydC P23886 CYDC_ECOLI cydC http://ecmdb.ca/proteins/P23886.xml ATP-binding/permease protein cydD P29018 CYDD_ECOLI cydD http://ecmdb.ca/proteins/P29018.xml tRNA sulfurtransferase P77718 THII_ECOLI thiI http://ecmdb.ca/proteins/P77718.xml Cysteine desulfuration protein sufE P76194 SUFE_ECOLI sufE http://ecmdb.ca/proteins/P76194.xml Aminopeptidase N P04825 AMPN_ECOLI pepN http://ecmdb.ca/proteins/P04825.xml Uncharacterized amino-acid ABC transporter ATP-binding protein yecC P37774 YECC_ECOLI yecC http://ecmdb.ca/proteins/P37774.xml Inner membrane amino-acid ABC transporter permease protein yecS P0AFT2 YECS_ECOLI yecS http://ecmdb.ca/proteins/P0AFT2.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Probable amino-acid metabolite efflux pump P31125 EAMA_ECOLI eamA http://ecmdb.ca/proteins/P31125.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Cysteine/O-acetylserine efflux protein P38101 EAMB_ECOLI eamB http://ecmdb.ca/proteins/P38101.xml Cystine-binding periplasmic protein P0AEM9 FLIY_ECOLI fliY http://ecmdb.ca/proteins/P0AEM9.xml Cysteinylglycine + Water > L-Cysteine + Glycine R00899 RXN-6622 Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-Cysteine RXN0-3 Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-Cysteine RXN0-3 L-Cysteine + SufSE sulfur acceptor complex > L-Alanine + SufSE with bound sulfur O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion R00897 ACSERLY-RXN L-Cysteine + Water > Hydrogen sulfide + Ammonium + Pyruvic acid Adenosine triphosphate + L-Cysteine + tRNA(Cys) + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + Pyrophosphate + L-Cysteinyl-tRNA(Cys) R03650 L-Cysteine + IscS sulfur acceptor protein > L-Alanine + IscS with bound sulfur Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate R00894 GLUTCYSLIG-RXN D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine > 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate R04231 P-PANTOCYSLIG-RXN L-Cysteine + O-Succinyl-L-homoserine <> L-Cystathionine + Hydrogen ion + Succinic acid R03260 O-SUCCHOMOSERLYASE-RXN L-Cysteine + Water <> Hydrogen sulfide + Pyruvic acid + Ammonia R00782 LCYSDESULF-RXN Adenosine triphosphate + L-Glutamate + L-Cysteine <> ADP + Phosphate + gamma-Glutamylcysteine R00894 L-Cysteine + alpha-Ketoglutarate <> 3-Mercaptopyruvic acid + DL-Glutamic acid R00896 O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid R00897 Cysteinylglycine + Water <> L-Cysteine + Glycine R00899 Cystathionine + Succinic acid <> O-Succinyl-L-homoserine + L-Cysteine R02508 o-acetyl-l-homoserine + L-Cysteine <> L-Cystathionine + Acetic acid R03217 O-Succinyl-L-homoserine + L-Cysteine <> L-Cystathionine + Succinic acid R03260 Adenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + Pyrophosphate + L-Cysteinyl-tRNA(Cys) R03650 Adenosine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Adenosine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine R04230 Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine R04231 O-Acetylserine + Thiosulfate + Thioredoxin + Hydrogen ion <> L-Cysteine + Sulfite + Thioredoxin disulfide + Acetic acid R04859 [Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine R07460 Oxoglutaric acid + L-Cysteine > L-Glutamate + 3-Mercaptopyruvic acid CYSTEINE-AMINOTRANSFERASE-RXN L-Cysteine + L-Glutamate + Adenosine triphosphate > Hydrogen ion + gamma-Glutamylcysteine + Phosphate + ADP GLUTCYSLIG-RXN L-Cysteine + Water > Pyruvic acid + Ammonia + Hydrogen sulfide + Hydrogen ion LCYSDESULF-RXN L-Cysteine + O-Succinyl-L-homoserine > Hydrogen ion + Succinic acid + L-Cystathionine O-SUCCHOMOSERLYASE-RXN L-Cysteine + a sulfur acceptor + Hydrogen ion L-Alanine + <i>S</i>-sulfanyl-[acceptor] RXN-12588 L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ion RXN0-3 L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ion RXN0-3 L-Cysteine + L-Cysteine-Desulfurases > L-Alanine + Persulfurated-L-cysteine-desulfurases RXN0-308 Cytidine triphosphate + (R)-4'-phosphopantothenate + L-Cysteine > Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine O-Acetylserine + Hydrogen sulfide > L-Cysteine + Acetic acid Adenosine triphosphate + L-Glutamate + L-Cysteine > ADP + Inorganic phosphate + gamma-Glutamylcysteine L-Cysteine + acceptor > L-Alanine + S-sulfanyl-acceptor O-Succinyl-L-homoserine + L-Cysteine > L-Cystathionine + Succinic acid Adenosine triphosphate + L-Cysteine + tRNA(Cys) > Adenosine monophosphate + Pyrophosphate + L-cysteinyl-tRNA(Cys) L-Cysteine + 'activated' tRNA > L-Serine + tRNA containing a thionucleotide L-Cysteine + 'Activated' tRNA <> L-Serine + tRNA containing a thionucleotide R03923 L-Cysteine + an [L-cysteine desulfurase] L-cysteine persulfide > an [L-cysteine desulfurase] L-cysteine persulfide + L-Alanine + L-Alanine PW_R002661 L-Cysteine + tRNA(Cys) + Adenosine triphosphate + Hydrogen ion > Pyrophosphate + Adenosine monophosphate + L-cysteinyl-tRNA(Cys) PW_R002824 O-Acetylserine > Hydrogen ion + Acetic acid + L-Cysteine PW_R002847 O-Acetylserine + Hydrogen sulfide > Hydrogen ion + Acetic acid + L-Cysteine PW_R002848 L-Cysteine > Hydrogen ion + Hydrogen sulfide + 2-Aminoacrylic acid PW_R003466 Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine + Cytidine monophosphate PW_R002991 D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + Hydrogen ion + 4-Phosphopantothenoylcysteine + Cytidine monophosphate PW_R003003 L-Glutamic acid + Adenosine triphosphate + L-Cysteine + L-Glutamate > Adenosine diphosphate + Phosphate + Hydrogen ion + gamma-Glutamylcysteine + ADP PW_R003052 L-Cysteine + Adenosine triphosphate + Water > ADP + Phosphate + Hydrogen ion PW_RCT000186 L-Cysteine > Hydrogen sulfide + Hydrogen ion + 2-aminoprop-2-enoate PW_R006145 O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion Adenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + Pyrophosphate O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid [Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine Cysteinylglycine + Water > L-Cysteine + Glycine Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate [Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate Luria-Bertani (LB) media Shake flask 204.0 uM true 45.0 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 816000 180000 Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602. 17535911