Purification and Characterization of N-Acetylglucosamine 6-Phosphate Deacetylase from Thermus caldophilus

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概要

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• 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℃ 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 Cu^<2+> but moderately activated by that of 1mM Mn^<2+> and Co^<2+>. 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.

• 公益社団法人日本生物工学会の論文
• 1999-09-25

著者

• Shin Hyun-jae

  Molecular Glycobiology Research Unit Korea Research Institute Of Bioscience And Biotechnology

• Lee Dae-sil

  Molecular Glycobiology Research Unit Korea Research Institute Of Bioscience And Biotechnology

• KIM MIKYUNG

  Molecular Glycobiology Research Unit, Korea Research Institute of Bioscience and Biotechnology

• Kim Mikyung

  Molecular Glycobiology Research Unit Korea Research Institute Of Bioscience And Biotechnology

関連論文

• Purification and Characterization of N-Acetylglucosamine 6-Phosphate Deacetylase from Thermus caldophilus

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