Enzymes
UniProtKB help_outline | 3 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
oxidized 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10004
Reactive part
help_outline
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline oxalate Identifier CHEBI:30623 (CAS: 338-70-5) help_outline Charge -2 Formula C2O4 InChIKeyhelp_outline MUBZPKHOEPUJKR-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
reduced 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10002
Reactive part
help_outline
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,006 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:30179 | RHEA:30180 | RHEA:30181 | RHEA:30182 | |
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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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Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica.
Daniel S.L., Pilsl C., Drake H.L.
Whole-cell and cell-extract experiments were performed to study the mechanism of oxalate metabolism in the acetogenic bacterium Moorella thermoacetica. In short-term, whole-cell assays, oxalate consumption was low unless cell suspensions were supplemented with CO(2), KNO(3), or Na(2)S(2)O(3). Cell ... >> More
Whole-cell and cell-extract experiments were performed to study the mechanism of oxalate metabolism in the acetogenic bacterium Moorella thermoacetica. In short-term, whole-cell assays, oxalate consumption was low unless cell suspensions were supplemented with CO(2), KNO(3), or Na(2)S(2)O(3). Cell extracts catalyzed the oxalate-dependent reduction of benzyl viologen. Oxalate consumption occurred concomitant to benzyl viologen reduction; when benzyl viologen was omitted, oxalate was not appreciably consumed. Based on benzyl viologen reduction, specific activities of extracts averaged 0.6 micromol oxalate oxidized min(-1) mg protein(-1). Extracts also catalyzed the formate-dependent reduction of NADP(+); however, oxalate-dependent reduction of NADP(+) was negligible. Oxalate- or formate-dependent reduction of NAD(+) was not observed. Addition of coenzyme A (CoA), acetyl-CoA, or succinyl-CoA to the assay had a minimal effect on the oxalate-dependent reduction of benzyl viologen. These results suggest that oxalate metabolism by M. thermoacetica requires a utilizable electron acceptor and that CoA-level intermediates are not involved. << Less
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Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate.
Pierce E., Becker D.F., Ragsdale S.W.
Moorella thermoacetica is an anaerobic acetogen, a class of bacteria that is found in the soil, the animal gastrointestinal tract, and the rumen. This organism engages the Wood-Ljungdahl pathway of anaerobic CO(2) fixation for heterotrophic or autotrophic growth. This paper describes a novel enzym ... >> More
Moorella thermoacetica is an anaerobic acetogen, a class of bacteria that is found in the soil, the animal gastrointestinal tract, and the rumen. This organism engages the Wood-Ljungdahl pathway of anaerobic CO(2) fixation for heterotrophic or autotrophic growth. This paper describes a novel enzyme, oxalate oxidoreductase (OOR), that enables M. thermoacetica to grow on oxalate, which is produced in soil and is a common component of kidney stones. Exposure to oxalate leads to the induction of three proteins that are subunits of OOR, which oxidizes oxalate coupled to the production of two electrons and CO(2) or bicarbonate. Like other members of the 2-oxoacid:ferredoxin oxidoreductase family, OOR contains thiamine pyrophosphate and three [Fe(4)S(4)] clusters. However, unlike previously characterized members of this family, OOR does not use coenzyme A as a substrate. Oxalate is oxidized with a k(cat) of 0.09 s(-1) and a K(m) of 58 μM at pH 8. OOR also oxidizes a few other 2-oxoacids (which do not induce OOR) also without any requirement for CoA. The enzyme transfers its reducing equivalents to a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. In conjunction with the well characterized Wood-Ljungdahl pathway, OOR should be sufficient for oxalate metabolism by M. thermoacetica, and it constitutes a novel pathway for oxalate metabolism. << Less