| glyoxylate dehydrogenase (acylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.17 | ||||||||
| CAS no. | 9028-96-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glyoxylate dehydrogenase (acylating) (EC 1.2.1.17) is an enzyme that catalyzes the chemical reaction
- glyoxylate + CoA + NADP oxalyl-CoA + NADPH + H
oxalyl-CoA + NADPH + HThe 3 substrates of this enzyme are glyoxylate, CoA, and NADP, whereas its 3 products are oxalyl-CoA, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glyoxylate:NADP+ oxidoreductase (CoA-oxalylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
- Quayle JR, Taylor GA (1961). "Carbon assimilation by Pseudomonas oxalaticus (OX1). 5. Purification and properties of glyoxylic dehydrogenase". Biochem. J. 78: 611–615.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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