glycine N-acyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.13 | ||||||||
CAS no. | 9029-95-2 | ||||||||
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 N-acyltransferase (GLYAT), also known as acyl-CoA:glycine N-acyltransferase (ACGNAT), (EC 2.3.1.13) is an enzyme that catalyzes the chemical reaction
- acyl-CoA + glycine CoA + N-acylglycine
Thus, the two substrates of this enzyme are acyl-CoA and glycine, whereas its two products are CoA and N-acylglycine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:glycine N-acyltransferase. Other names in common use include glycine acyltransferase, and glycine-N-acylase.
This enzyme plays a prominent role in converting benzoic acid (benzoate) into hippuric acid (N-benzoylglycine). Benzoic acid is metabolized by butyrate-CoA ligase into an intermediate product, benzoyl-CoA,[1] which is then metabolized by glycine N-acyltransferase into hippuric acid.[2]
References
- ↑ "Substrate/Product". butyrate-CoA ligase. BRENDA. Technische Universität Braunschweig. Retrieved 7 May 2014.
- ↑ "Substrate/Product". glycine N-acyltransferase. BRENDA. Technische Universität Braunschweig. Retrieved 7 May 2014.
- Nandi DL, Lucas SV, Webster LT (1979). "Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization". J. Biol. Chem. 254 (15): 7230–7. PMID 457678.
- SCHACHTER D, TAGGART JV (1954). "Glycine N-acylase: purification and properties". J. Biol. Chem. 208 (1): 263–75. PMID 13174534.
- Webster LT, Siddiqui UA, Lucas SV, Strong JM, Mieyal JJ (1976). "Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man". J. Biol. Chem. 251 (11): 3352–8. PMID 931988.