Biology:Glutaryl-7-aminocephalosporanic-acid acylase
| Glutaryl-7-aminocephalosporanic-acid acylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.93 | ||||||||
| 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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In enzymology, a glutaryl-7-aminocephalosporanic-acid acylase (EC 3.5.1.93) is an enzyme that catalyzes the chemical reaction
- (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] (7R)-7-aminocephalosporanate + glutarate
Thus, the two substrates of this enzyme are (7R)-7-(4-carboxybutanamido)cephalosporanate and H2O, whereas its two products are (7R)-7-aminocephalosporanate and glutarate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase. Other names in common use include 7beta-(4-carboxybutanamido)cephalosporanic acid acylase, cephalosporin C acylase, glutaryl-7-ACA acylase, CA, GCA, GA, cephalosporin acylase, glutaryl-7-aminocephalosporanic acid acylase, and GL-7-ACA acylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References
- Shimomura K; Saito, Y; Fujimura, T; Sasaki, H; Noguchi, Y; Yamada, H; Niwa, M; Shimomura, K (1995). "High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176". Eur. J. Biochem. 230 (2): 773–778. doi:10.1111/j.1432-1033.1995.0773h.x. PMID 7607251.
- "Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176". Acta Crystallogr. D 56 (Pt 4): 458–459. doi:10.1107/S0907444900000718. PMID 10739919.
- "Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase". Biotechnol. Bioeng. 70 (2): 239–244. 2000. doi:10.1002/1097-0290(20001020)70:2<239::AID-BIT13>3.0.CO;2-I. PMID 10972935.
- "Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp GK16". J. Struct. Biol. 131 (1): 79–81. 2000. doi:10.1006/jsbi.2000.4256. PMID 10945972.
- "The 2.0 A crystal structure of cephalosporin acylase". Structure. Fold. Des. 8 (10): 1059–1068. 2000. doi:10.1016/S0969-2126(00)00505-0. PMID 11080627.
- G; Zeng, R; Ding, X; Mao, X; Ding, Y; Rao, Z; Xie, Y; Jiang, W et al. (2002). "Affinity alkylation of the Trp-B4 residue of the beta -subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp 130". J. Biol. Chem. 277 (12): 10256–10264. doi:10.1074/jbc.M108683200. PMID 11782466.
- "Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation". Biochemistry 42 (14): 4084–4093. 2003. doi:10.1021/bi027181x. PMID 12680762.
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