| glycine dehydrogenase (cytochrome) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.2.1 | ||||||||
| CAS no. | 9075-55-2 | ||||||||
| 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 glycine dehydrogenase (cytochrome) (EC 1.4.2.1) is an enzyme that catalyzes the chemical reaction
- glycine + H2O + 2 ferricytochrome c glyoxylate + NH3 + 2 ferrocytochrome c + 2 H
glyoxylate + NH3 + 2 ferrocytochrome c + 2 HThe 3 substrates of this enzyme are glycine, H2O, and ferricytochrome c, whereas its 4 products are glyoxylate, NH3, ferrocytochrome c, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is glycine:ferricytochrome-c oxidoreductase (deaminating). This enzyme is also called glycine---cytochrome c reductase. This enzyme participates in glycine, serine and threonine metabolism.
References
- Sanders HK, Becker GE, Nason A (1972). "Glycine-cytochrome c reductase from Nitrobacter agilis". J. Biol. Chem. 247 (7): 2015–25. PMID 5016640.
| CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1: NAD/NADP acceptor | |
| 1.4.3: oxygen acceptor | |
| 1.4.4: disulfide acceptor | |
| 1.4.99: other acceptors | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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