| glycolaldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.21 | ||||||||
| CAS no. | 37250-89-8 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glycolaldehyde dehydrogenase (EC 1.2.1.21) is an enzyme that catalyzes the chemical reaction
- glycolaldehyde + NAD + H2O glycolate + NADH + H
glycolate + NADH + HThe 3 substrates of this enzyme are glycolaldehyde, NAD, and H2O, whereas its 3 products are glycolate, NADH, 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 glycolaldehyde:NAD+ oxidoreductase. This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2HG2, 2ILU, and 2IMP.
References
- Davies DD (1960). "The purification and properties of glycolaldehyde dehydrogenase". J. Exp. Bot. 11 (3): 289–295. doi:10.1093/jxb/11.3.289.
| 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 | |
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