Biology:Glycine oxidase
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Short description: Class of enzymes
Glycine oxidase | |||||||||
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Glycine oxidase tetramer, Geobacillus kaustophilus | |||||||||
Identifiers | |||||||||
EC number | 1.4.3.19 | ||||||||
CAS number | 39307-16-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glycine oxidase (EC 1.4.3.19) is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating).[1][2] This enzyme catalyses the following chemical reaction
- glycine + H2O + O2 [math]\displaystyle{ \rightleftharpoons }[/math] glyoxylate + NH3 + H2O2 (overall reaction)
- (1a) glycine + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2-iminoacetate + H2O2
- (1b) 2-iminoacetate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] glyoxylate + NH3
This flavoenzyme containing non-covalently bound FAD.
References
- ↑ "Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein". The Journal of Biological Chemistry 277 (9): 6985–93. March 2002. doi:10.1074/jbc.M111095200. PMID 11744710.
- ↑ "Purification and characterization of a novel glycine oxidase from Bacillus subtilis". FEBS Letters 438 (3): 263–6. November 1998. doi:10.1016/s0014-5793(98)01313-1. PMID 9827558.
External links
- Glycine+oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Glycine oxidase.
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