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Title 

Characterization of a thermostable D-stereospecific alanine amidase from Brevibacillus borstelensis BCS-1

Authors 

Dae Heoun BackSeok Joon KwonSeung Pyo HongMi Sun KwakMi Hwa LeeJae Jun SongSeung Goo LeeK H YoonMoon Hee Sung

Publisher 

American Society for Microbiology

Issue Date 

2003

Citation 

Applied and Environmental Microbiology, vol. 69, no. 2, pp. 980-986

Keywords 

amino acidsgene encodingalanine amidaseamidecobaltdextro alaninamidedithiothreitoledetic acidmanganesemercaptoethanol

Abstract 

A gene encoding a new thermostable D-stereospecific alanine amidase from the thermophile Brevibacillus borstelensis BCS-1 was cloned and sequenced. The molecular mass of the purified enzyme was estimated to be 199 kDa after gel filtration chromatography and about 30 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that the enzyme could be composed of a hexamer with identical subunits. The purified enzyme exhibited strong amidase activity towards D-amino acid-containing aromatic, aliphatic, and branched amino acid amides yet exhibited no enzyme activity towards L-amino acid amides, D-amino acid-containing peptides, and NH2-terminally protected amino acid amides. The optimum temperature and pH for the enzyme activity were 85°C and 9.0, respectively. The enzyme remained stable within a broad pH range from 7.0 to 10.0. The enzyme was inhibited by dithiothreitol, 2-mercaptoethanol, and EDTA yet was strongly activated by Co2+ and Mn2+. The kcat/Km for D-alaninamide was measured as 544.4 ± 5.5 mM-1 min-1 at 50°C with 1 mM Co2+.

ISSN 

0099-2240

Link 

http://dx.doi.org/10.1128/AEM.69.2.980-986.2003

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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