Glutaryl-7-aminocephalosporanic-acid acylase

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.
Kinoshita T, Tada T, Saito Y, Ishii Y, Sato A, Murata M. "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.
Monti D, Carrea G, Riva S, Baldaro E, Frare G (2000). "Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase". Biotechnol. Bioeng. 70 (2): 239–244. doi:10.1002/1097-0290(20001020)70:2<239::AID-BIT13>3.0.CO;2-I. PMID 10972935.
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 (1): 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 (10): 1059–1068. 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; Zhao, 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 (12): 10256–10264. 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 (14): 4084–4093. doi:10.1021/bi027181x. PMID 12680762.

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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