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, Ichiro; Fukagawa, Masafumi; Tsumura, Mana; Iwami, Morita; Ono, Hiroki; Kojo, Hitoshi; Kohsaka, Masanobu; Ueda, Yoshio; Imanaka, Hiroshi

doi:10.1128/jb.173.24.7848-7855.1991

Cited by 38 publications

(13 citation statements)

References 26 publications

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“…The enzyme has a small cap domain and an extensive C-terminal domain that is largely ␤-stranded. The enzyme is homologous to one other ␤-lactam antibiotic acylase, glutaryl 7-aminocephalosporanic acid acylase from Bacillus laterosporus (16), which is expected to have a similar structure. These results define a class of ␤-lactam antibiotic acylases that is clearly different from other known ␤-lactam antibiotic acylases that belong to the Ntnhydrolase family.…”

Section: Expression Of Aeh In E Coli With N-terminal Hismentioning

confidence: 99%

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Polderman-Tijmes¹,

Jekel²,

Jeronimus-Stratingh³

et al. 2002

Journal of Biological Chemistry

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The ␣-amino acid ester hydrolase from Acetobacter turbidans ATCC 9325 is capable of hydrolyzing and synthesizing the side chain peptide bond in ␤-lactam antibiotics. Data base searches revealed that the enzyme contains an active site serine consensus sequence Gly-X-Ser-Tyr-X-Gly that is also found in X-prolyl dipeptidyl aminopeptidase. The serine hydrolase inhibitor p-nitrophenyl-p-guanidino-benzoate appeared to be an active site titrant and was used to label the ␣-amino acid ester hydrolase. Electrospray mass spectrometry and tandem mass spectrometry analysis of peptides from a to an alanine almost fully inactivated the enzyme, whereas mutation of the other residues did not seriously affect the enzyme activity. Circular dichroism measurements showed that the inactivation was not caused by drastic changes in the tertiary structure. Therefore, we conclude that the catalytic domain of the ␣-amino acid ester hydrolase has an ␣/␤-hydrolase fold structure with a catalytic triad of Ser 205 , Asp 338 , and His 370 . This distinguishes the ␣-amino acid ester hydrolase from the Ntnhydrolase family of ␤-lactam antibiotic acylases.

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Section: Expression Of Aeh In E Coli With N-terminal Hismentioning

confidence: 99%

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Polderman-Tijmes¹,

Jekel²,

Jeronimus-Stratingh³

et al. 2002

Journal of Biological Chemistry

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“…on optimization of recombinant E. coli expressing AEH and GA. 14,15) In addition, there have been no reports that the phoC promoter has been repressed by means of higher concentrations of glucose. Though the reason is not clear, the above results suggest that a higher glucose feeding rate is likely to inhibit the expression of SAET.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic Production ofL-Alanyl-L-glutamine by RecombinantE. coliExpressing α-Amino Acid Ester Acyltransferase fromSphingobacterium siyangensis

Hirao

Mihara

Kira

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…In comparison, the one-step enzymatic method is efficient and has been studied intensively [2]. Researchers separated CPC acylase from the micro-organisms which could convert CPC into 7-ACA directly [5][6][7][8][9]. But, the application of the wild strain was inconvenient [3] and the question was that CPC acylases *Address correspondence to this author at the Key Laboratory of Ecology and Biological Resources in Yarkand Oasis at Universities under the Education Department of Xinjiang Uygur Autonomous Region, Department of Biological Science, Kashi Normal College, No.29.…”

Section: Introductionmentioning

confidence: 99%

Modeling and Experimental Analysis of Cephalosporin C Acylase and Its Mutant

Ren¹

2013

TOBIOTJ

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7-amino cephalosporanic acid (7-ACA) is the crucial intermediate for the synthesis of semi-synthetic antibiotics, which is currently prepared by two-step biocatalysis using D-amino acid oxidase and glutaryl-7-amino cephalosporanic acid acylase (GL-7-ACA acylase) starting from cephalosporin C (CPC). Compared with the two-step enzymatic method, one-step method is more efficient and economical. But, the available Cephalosporin C acylase (CPC acylase) always take glutaryl-7-amino cephalosporanic acid (GL-7-ACA) as their primary substrate, and have low catalytic activities towards CPC to be used in industry. We investigated the catalytic mechanism of CPC acylase by the sequence alignment, homology modeling, and active site analysis to a series of CPC acylases from Pseudomonas where some effective mutations have been reported for activity enhancement. Two CPC acylases coded by the genes acyII and S12 are studied intensively for the interaction between the amino acid residues in the activity region and the substrate CPC based upon the complex structure obtained from the homology modeling and molecular docking. Furthermore, the catalytic parameters of the two CPC acylases were measured experimentally in order to corroborate the modeling analysis and propose potential designing strategy for improvement of enzymic activity.

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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

Cited by 38 publications

References 26 publications

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Enzymatic Production ofL-Alanyl-L-glutamine by RecombinantE. coliExpressing α-Amino Acid Ester Acyltransferase fromSphingobacterium siyangensis

Modeling and Experimental Analysis of Cephalosporin C Acylase and Its Mutant

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