A new d-aminoacylase from Defluvibacter sp. A 131-3

A new d-aminoacylase from Defluvibacter sp. A 131-3

A new d-aminoacylase was found from Defluvibacter sp. A 131-3. It was purified to homogeneity with an overall yield of 37%. This enzyme was specific to N-acyl- d-amino acids, and the activity on N-acetyl- d-valine was higher than that of the other N-acyl- d-amino acids. The enzyme activity was inhib...

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Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Vol. 30; no. 3; pp. 159 - 165
Main Authors: Kumagai, Shinya, Kobayashi, Masayuki, Yamaguchi, Seiki, Kanaya, Takami, Motohashi, Rie, Isobe, Kimiyasu
Format: Journal Article
Language:English
Published: Amsterdam Elsevier B.V 16-08-2004
Elsevier Science
Subjects:
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
d-aminoacylase
d-valine
Defluvibacter
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Defluvibacter
d-aminoacylase
d-valine
Enzyme
Valine
D-valine
Hydrolases
Bacteria
D-aminoacylase
N-Acyl-D-amino-acid deacylase
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Description
Summary:A new d-aminoacylase was found from Defluvibacter sp. A 131-3. It was purified to homogeneity with an overall yield of 37%. This enzyme was specific to N-acyl- d-amino acids, and the activity on N-acetyl- d-valine was higher than that of the other N-acyl- d-amino acids. The enzyme activity was inhibited with CoCl 2, NiCl 2, MnCl 2, and ZnCl 2. Optimum pH and temperature were 8.0 and 37 °C, respectively. This enzyme is monomeric with a molecular mass of 56 kDa and an isoelectric point of 5.3. The NH 2-terminal sequence similarity was less than 30% of the previously reported d-aminoacylase. This enzyme has great potential for production of d-valine.
ISSN:1381-1177
1873-3158
DOI:10.1016/j.molcatb.2004.04.006