In enzymology, a glycine dehydrogenase (cytochrome) (EC 1.4.2.1) is an enzyme that catalyzes the chemical reaction
glycine dehydrogenase (cytochrome) | |||||||||
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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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- glycine + H2O + 2 ferricytochrome c glyoxylate + NH3 + 2 ferrocytochrome c + 2 H+
The 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
edit- Sanders HK, Becker GE, Nason A (1972). "Glycine-cytochrome c reductase from Nitrobacter agilis". J. Biol. Chem. 247 (7): 2015–25. PMID 5016640.