2.02012-05-31 14:26:19 -06002015-06-03 17:19:16 -0600ECMDB20078M2MDB0009273,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene3,4-dihydro-3-hydroxy-4-s-glutathionyl bromobenzene belongs to the class of Peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. (inferred from compound structure)(2S)-2-amino-5-(2R)-3-(4-bromo-6-Hydroxycyclohexa-2,4-dien-1-yl)sulfanyl-1-(carboxymethylamino)-1-oxopropan-2-ylamino-5-oxopentanoate(2S)-2-amino-5-(2R)-3-(4-bromo-6-hydroxycyclohexa-2,4-dien-1-yl)sulfanyl-1-(carboxymethylamino)-1-oxopropan-2-ylamino-5-oxopentanoic acid(2S)-2-amino-5-(2R)-3-(4-bromo-6-Hydroxycyclohexa-2,4-dien-1-yl)sulphanyl-1-(carboxymethylamino)-1-oxopropan-2-ylamino-5-oxopentanoate(2S)-2-amino-5-(2R)-3-(4-bromo-6-Hydroxycyclohexa-2,4-dien-1-yl)sulphanyl-1-(carboxymethylamino)-1-oxopropan-2-ylamino-5-oxopentanoic acidL-g-Glutamyl-S-(4-bromo-6-hydroxy-2,4-cyclohexadien-1-yl)-L-cysteinylglycineL-gamma-Glutamyl-S-(4-bromo-6-hydroxy-2,4-cyclohexadien-1-yl)-L-cysteinylglycineL-γ-Glutamyl-S-(4-bromo-6-hydroxy-2,4-cyclohexadien-1-yl)-L-cysteinylglycineC16H22BrN3O7S480.331479.03618341(2S)-2-amino-4-{[(1R)-2-[(4-bromo-6-hydroxycyclohexa-2,4-dien-1-yl)sulfanyl]-1-[(carboxymethyl)-C-hydroxycarbonimidoyl]ethyl]-C-hydroxycarbonimidoyl}butanoic acidC16H22brN3O7S[H][C@](N)(CCC(O)=N[C@@]([H])(CSC1([H])C=CC(Br)=CC1([H])O)C(O)=NCC(O)=O)C(O)=OInChI=1S/C16H22BrN3O7S/c17-8-1-3-12(11(21)5-8)28-7-10(15(25)19-6-14(23)24)20-13(22)4-2-9(18)16(26)27/h1,3,5,9-12,21H,2,4,6-7,18H2,(H,19,25)(H,20,22)(H,23,24)(H,26,27)/t9-,10-,11?,12?/m0/s1WIPMNDWTVDZAHE-JYBOHDQNSA-NCytoplasmPeriplasmlogp-1.75logs-3.73solubility8.88e-02 g/llogp-2.4pka_strongest_acidic1.86pka_strongest_basic9.54iupac(2S)-2-amino-4-{[(1R)-2-[(4-bromo-6-hydroxycyclohexa-2,4-dien-1-yl)sulfanyl]-1-[(carboxymethyl)-C-hydroxycarbonimidoyl]ethyl]-C-hydroxycarbonimidoyl}butanoic acidaverage_mass480.331mono_mass479.03618341smiles[H][C@](N)(CCC(O)=N[C@@]([H])(CSC1([H])C=CC(Br)=CC1([H])O)C(O)=NCC(O)=O)C(O)=OformulaC16H22BrN3O7SinchiInChI=1S/C16H22BrN3O7S/c17-8-1-3-12(11(21)5-8)28-7-10(15(25)19-6-14(23)24)20-13(22)4-2-9(18)16(26)27/h1,3,5,9-12,21H,2,4,6-7,18H2,(H,19,25)(H,20,22)(H,23,24)(H,26,27)/t9-,10-,11?,12?/m0/s1inchikeyWIPMNDWTVDZAHE-JYBOHDQNSA-Npolar_surface_area186.03refractivity106.82polarizability42.71rotatable_bond_count11acceptor_count10donor_count6physiological_charge-2formal_charge0glutathione metabolism IIIThe 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.
PW002018Metabolic2,3-dihydroxybenzoate biosynthesisPWY-5901Specdb::CMs34262Specdb::CMs48166Specdb::CMs161926Specdb::CMs161928Specdb::CMs161930Specdb::CMs161932Specdb::CMs161934Specdb::CMs161937Specdb::CMs161939Specdb::CMs170459Specdb::CMs280382Specdb::NmrOneD57772Specdb::NmrOneD57773Specdb::NmrOneD57774Specdb::NmrOneD57775Specdb::NmrOneD57776Specdb::NmrOneD57777Specdb::NmrOneD57778Specdb::NmrOneD57779Specdb::NmrOneD57780Specdb::NmrOneD57781Specdb::NmrOneD57782Specdb::NmrOneD57783Specdb::NmrOneD57784Specdb::NmrOneD57785Specdb::NmrOneD57786Specdb::NmrOneD57787Specdb::NmrOneD57788Specdb::NmrOneD57789Specdb::NmrOneD57790Specdb::NmrOneD57791Specdb::MsMs24785Specdb::MsMs24786Specdb::MsMs24787Specdb::MsMs31343Specdb::MsMs31344Specdb::MsMs313451195406610128361C14847DIHYDRO-DIOH-BENZOATEKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510Glutathione S-transferaseP0A9D2GST_ECOLIgsthttp://ecmdb.ca/proteins/P0A9D2.xmlGSH-dependent disulfide bond oxidoreductaseP77526yfcGhttp://ecmdb.ca/proteins/P77526.xmlBromobenzene-3,4-oxide + Glutathione <> 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzeneR07069Bromobenzene-3,4-oxide + Glutathione < 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzenePW_R005900