Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase from Thermus caldophilus

Cited 4 time in scopus
Metadata Downloads
Title
Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase from Thermus caldophilus
Author(s)
Hyun Jae Shin; Mi Kyung Kim; Dae Sil Lee
Bibliographic Citation
Journal of Bioscience and Bioengineering, vol. 88, no. 3, pp. 319-322
Publication Year
1999
Abstract
N-Acetylglucosamine 6-phosphate deacetylase [EC 3.5.1.25] was purified and biochemically characterized from an extreme thermophile, Thermus caldophilus GK24. The optimum temperature and pH of the enzyme were 80°C and 7.5, respectively. The enzyme is a tetramer composed of identical 45 kDa subunits. The N-terminal amino acid sequence of the purified enzyme was determined to be MSVDLKTLHRRHVLTP. It hydrolyzed GlcNAc-6-P, but not GlcNAc- 1-P or chitin oligosaccharides. The deacetylase activity was completely inhibited by the addition of 1 mM Cu2+, but moderately activated by that of 1 mM Mn2+ and Co2+. Within 2 h of reaction, 2 mM GlcNAc-6-P was completely hydrolyzed to GlcN-6-P and acetate by the action of the deacetylase.
Keyword
N-acetylglucosamine 6-phosphate deacetylaseThermus caldophilusnagA gene
ISSN
1389-1723
Publisher
Soc Bioscience Bioengineering Japan
DOI
http://dx.doi.org/10.1016/S1389-1723(00)80017-1
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.