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Title 

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

Authors 

Hyun Jae ShinMi Kyung KimDae Sil Lee

Publisher 

Elsevier

Issue Date 

1999

Citation 

Journal of Bioscience and Bioengineering, vol. 88, no. 3, pp. 319-322

Keywords 

N-acetylglucosamine 6-phosphate deacetylaseThermus caldophilusnagA gene

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.

ISSN 

1389-1723

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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