Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
[mycoredoxin]-L-cysteine
Identifier
RHEA-COMP:13766
Reactive part
help_outline
- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 123 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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[mycoredoxin]-S-mycothiol-L-cysteine
Identifier
RHEA-COMP:13767
Reactive part
help_outline
- Name help_outline S-mycothiol-L-cysteine residue Identifier CHEBI:138035 Charge 0 Formula C20H33N3O13S2 SMILEShelp_outline C([C@H](CSSC[C@H](N*)C(=O)*)NC(=O)C)(N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[C@@H]2[C@@H]([C@@H]([C@H]([C@@H]([C@H]2O)O)O)O)O)CO)O)O)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline arsenite Identifier CHEBI:29242 Charge -1 Formula AsH2O3 InChIKeyhelp_outline AQLMHYSWFMLWBS-UHFFFAOYSA-N SMILEShelp_outline O[As](O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:54036 | RHEA:54037 | RHEA:54038 | RHEA:54039 | |
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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.