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Chemical Compound Review:

Glutaryl-7-aca (6R,7S)-3-(acetyloxymethyl)- 7-(4...

Synonyms: SureCN569055, Gl-7-Aca, AG-E-89184, CHEBI:41425, AC1L9JTQ, ...

Monti, D. et al., Alonso-Morales, N. et al., Kwon, T.H. et al., Aramori, I. et al., Yau, M.H. et al., et al.

Pollegioni, Lorenzi, Rosini, Marcone, Molla, Verga, Cabri, Pilone, Suzuki, Miwa, Ishihara, Kumagai, Isoai, Kimura, Reichert, Schörgendorfer, Nikaido, Tohda, Giga-Hama, Mutoh, Kumagai, Khang, Kim, Hah, Hwangbo, Kang,

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Disease relevance of Gl-7-Aca

In the present study, glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas sp. strain 130 (CA130) was mutated to improve its enzymatic activity and stability [1].
Expression of the gene for glutaryl 7-ACA acylase was performed in both E. coli and Bacillus subtilis [2].

High impact information on Gl-7-Aca

In total, 24 out of 41 plate-selected mutants were found to have a significantly improved ratio of adipyl-7-ADCA versus glutaryl-7-ACA hydrolysis [3].
Two binary structures in complex with glutaryl-7-ACA (the most favored substrate of CAs) and glutarate (side chain of glutaryl-7-ACA) were determined, and they revealed the detailed interactions of glutaryl-7-ACA with the active site residues (Y [4].
J1 acylase, a glutaryl-7-aminocephalosporanic acid acylase (GCA) isolated from Bacillus laterosporus J1, has been conventionally grouped as the only member of class V GCA, although its amino acid sequence shares less than 10% identity with members of other classes of GCA [5].
Starting from a known glutaryl-7-amino cephalosporanic acid acylase as the protein scaffold, an acylase gene optimized for expression in Escherichia coli and for molecular biology manipulations was designed [6].
This substitution enabled gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocephalosporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins [7].

Chemical compound and disease context of Gl-7-Aca

Glutaryl-7-aminocephalosporanicacid acylase from Pseudomonas sp. GK16 produces glutaryl-7-aminocephalosporanic acid, a key intermediate for the synthesis of cephem antibiotics [8].

Biological context of Gl-7-Aca

The gene for the glutaryl 7-ACA acylase was cloned with pHSG298 in Escherichia coli JM109, and the nucleotide sequence was determined by the M13 dideoxy chain termination method [2].
Several mutations cause a substrate specificity shift from the preferred substrate of the enzyme, glutaryl-7-ACA, towards the desired substrate, adipyl-7-ADCA [9].
A clone, ASP327-10, transformed with plasmid vector, pTL2M5DAO, expressed catalytically active DAO in the presence of G418, and converted Cephalosprin C to alpha-ketoadipyl-7-cephalosporanic acid (KA-7-ACA) and glutaryl-7-aminocephalosporanic acid (GL-7-ACA) [10].
A batch of the immobilized industrial biocatalyst glutaryl-7-ACA acylase (GA), one of the two enzymes involved in the biotransformation of cephalosporin C (CefC) into 7-aminocephalosporanic acid (7-ACA), was characterized [11].

Associations of Gl-7-Aca with other chemical compounds

The immobilizaton of the enzyme glutaryl-7-aminocephalosporanic acid acylase (GA) was performed via ionic adsorption onto several supports: a new anionic exchange resin, based on the coating of Sepabeads internal surfaces with polyethyleneimine (PEI) of different molecular weights, and conventional EC-Q1A-Sepabeads and DEAE-agarose [12].

Gene context of Gl-7-Aca

Following the complete conversion of a 75 mM solution of CefC into glutaryl-7-ACA catalyzed by an immobilized D-amino acid oxidase (DAAO), immobilized GA was used for the transformation of this intermediate into the final product 7-ACA [11].

Analytical, diagnostic and therapeutic context of Gl-7-Aca

Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16 [8].
The purity of the final product, glutaryl-7-aminocephalosporanic acid, was confirmed to be 99.77% by high-performance liquid chromatography (HPLC) analysis [13].
Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability [14].

References

Improving the activity and stability of GL-7-ACA acylase CA130 by site-directed mutagenesis. Zhang, W., Liu, Y., Zheng, H., Yang, S., Jiang, W. Appl. Environ. Microbiol. (2005) [Pubmed]
Cloning and nucleotide sequencing of a novel 7 beta-(4-carboxybutanamido)cephalosporanic acid acylase gene of Bacillus laterosporus and its expression in Escherichia coli and Bacillus subtilis. Aramori, I., Fukagawa, M., Tsumura, M., Iwami, M., Ono, H., Kojo, H., Kohsaka, M., Ueda, Y., Imanaka, H. J. Bacteriol. (1991) [Pubmed]
Altering the substrate specificity of cephalosporin acylase by directed evolution of the Beta -subunit. Otten, L.G., Sio, C.F., Vrielink, J., Cool, R.H., Quax, W.J. J. Biol. Chem. (2002) [Pubmed]
Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for post-translational modification. Kim, S., Kim, Y. J. Biol. Chem. (2001) [Pubmed]
J1 acylase, a glutaryl-7-aminocephalosporanic acid acylase from Bacillus laterosporus J1, is a member of the alpha/beta-hydrolase fold superfamily. Yau, M.H., Wang, J., Tsang, P.W., Fong, W.P. FEBS Lett. (2006) [Pubmed]
Evolution of an acylase active on cephalosporin C. Pollegioni, L., Lorenzi, S., Rosini, E., Marcone, G.L., Molla, G., Verga, R., Cabri, W., Pilone, M.S. Protein Sci. (2005) [Pubmed]
A single amino acid substitution converts gamma-glutamyltranspeptidase to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase). Suzuki, H., Miwa, C., Ishihara, S., Kumagai, H. Appl. Environ. Microbiol. (2004) [Pubmed]
Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S., Kim, K.H. J. Struct. Biol. (2000) [Pubmed]
Analysis of a substrate specificity switch residue of cephalosporin acylase. Sio, C.F., Otten, L.G., Cool, R.H., Quax, W.J. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
Production of D-amino acid oxidase (DAO) of Trigonopsis variabilis in Schizosaccharomyces pombe and the characterization of biocatalysts prepared with recombinant cells. Isoai, A., Kimura, H., Reichert, A., Schörgendorfer, K., Nikaido, K., Tohda, H., Giga-Hama, Y., Mutoh, N., Kumagai, H. Biotechnol. Bioeng. (2002) [Pubmed]
Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Monti, D., Carrea, G., Riva, S., Baldaro, E., Frare, G. Biotechnol. Bioeng. (2000) [Pubmed]
Reversible immobilization of glutaryl acylase on sepabeads coated with polyethyleneimine. Alonso-Morales, N., López-Gallego, F., Betancor, L., Hidalgo, A., Mateo, C., Fernández-Lafuente, R., Guisán, J.M. Biotechnol. Prog. (2004) [Pubmed]
Fusion protein of Vitreoscilla hemoglobin with D-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C. Khang, Y.H., Kim, I.W., Hah, Y.R., Hwangbo, J.H., Kang, K.K. Biotechnol. Bioeng. (2003) [Pubmed]
Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability. Park, S.W., Lee, J.W., Hong, S.I., Kim, S.W. Appl. Biochem. Biotechnol. (2003) [Pubmed]

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