Glutaryl-7-aminocephalosporanic-acid acylase

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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 $\rightleftharpoons$ (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.

[edit] References

IUBMB entry for 3.5.1.93
BRENDA references for 3.5.1.93 (Recommended.)
PubMed references for 3.5.1.93
PubMed Central references for 3.5.1.93
Google Scholar references for 3.5.1.93
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Kwon TH, Rhee S, Lee YS, Park SS, Kim KH (2000). "Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp GK16". J. Struct. Biol. 131: 79–81. doi:10.1006/jsbi.2000.4256. PMID 10945972.
Kim Y, Yoon K, Khang Y, Turley S, Hol WG (2000). "The 2.0 A crystal structure of cephalosporin acylase". Structure. Fold. Des. 8: 1059–68. doi:10.1016/S0969-2126(00)00505-0. PMID 11080627.
G (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: 10256–64. doi:10.1074/jbc.M108683200. PMID 11782466.
Kim JK, Yang IS, Rhee S, Dauter Z, Lee YS, Park SS, Kim KH (2003). "Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation". Biochemistry. 42: 4084–93. doi:10.1021/bi027181x. PMID 12680762.