Cited 24 time in
- Characterization of a thermostable D-stereospecific alanine amidase from Brevibacillus borstelensis BCS-1
- Dae Heoun Back; Seok Joon Kwon; Seung Pyo Hong; Mi Sun Kwak; Mi Hwa Lee; Jae Jun Song; Seung Goo Lee; K H Yoon; Moon Hee Sung
- Bibliographic Citation
- Applied and Environmental Microbiology, vol. 69, no. 2, pp. 980-986
- Publication Year
- 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+.
- Amer Soc Microb
- Appears in Collections:
- Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.