Enzymes
| UniProtKB help_outline | 4 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline arsenate Identifier CHEBI:48597 Charge -2 Formula AsHO4 InChIKeyhelp_outline DJHGAFSJWGLOIV-UHFFFAOYSA-L SMILEShelp_outline O[As]([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline mycothiol Identifier CHEBI:16768 (Beilstein: 9308053; CAS: 192126-76-4) help_outline Charge 0 Formula C17H30N2O12S InChIKeyhelp_outline MQBCDKMPXVYCGO-FQBKTPCVSA-N SMILEShelp_outline CC(=O)N[C@@H](CS)C(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline arseno-mycothiol Identifier CHEBI:59655 Charge -2 Formula C17H29AsN2O15S InChIKeyhelp_outline UFFVRAZTLALLGR-FQBKTPCVSA-L SMILEShelp_outline CC(=O)N[C@@H](CS[As]([O-])([O-])=O)C(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:27349 | RHEA:27350 | RHEA:27351 | RHEA:27352 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange.
Ordonez E., Van Belle K., Roos G., De Galan S., Letek M., Gil J.A., Wyns L., Mateos L.M., Messens J.
We identified the first enzymes that use mycothiol and mycoredoxin in a thiol/disulfide redox cascade. The enzymes are two arsenate reductases from Corynebacterium glutamicum (Cg_ArsC1 and Cg_ArsC2), which play a key role in the defense against arsenate. In vivo knockouts showed that the genes for ... >> More
We identified the first enzymes that use mycothiol and mycoredoxin in a thiol/disulfide redox cascade. The enzymes are two arsenate reductases from Corynebacterium glutamicum (Cg_ArsC1 and Cg_ArsC2), which play a key role in the defense against arsenate. In vivo knockouts showed that the genes for Cg_ArsC1 and Cg_ArsC2 and those of the enzymes of the mycothiol biosynthesis pathway confer arsenate resistance. With steady-state kinetics, arsenite analysis, and theoretical reactivity analysis, we unraveled the catalytic mechanism for the reduction of arsenate to arsenite in C. glutamicum. The active site thiolate in Cg_ArsCs facilitates adduct formation between arsenate and mycothiol. Mycoredoxin, a redox enzyme for which the function was never shown before, reduces the thiol-arseno bond and forms arsenite and a mycothiol-mycoredoxin mixed disulfide. A second molecule of mycothiol recycles mycoredoxin and forms mycothione that, in its turn, is reduced by the NADPH-dependent mycothione reductase. Cg_ArsCs show a low specificity constant of approximately 5 m(-1) s(-1), typically for a thiol/disulfide cascade with nucleophiles on three different molecules. With the in vitro reconstitution of this novel electron transfer pathway, we have paved the way for the study of redox mechanisms in actinobacteria. << Less
J. Biol. Chem. 284:15107-15116(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.