Stabilization of Flavobacterium meningosepticum Glycerol Kinase by Introduction of a Hydrogen Bond(Biochemistry & Molecular Biology)

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概要

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• The thermostability of Flavobacterium meningosepticum glycerol kinase was increased by the change from Ser329 to Asp [Protein Eng., 14, 663-667 (2001)]. Based on a three-dimensional structure model of the mutant, we have postulated that a new charged-neutral hydrogen bond was formed between Asp329 and Ser414, and the formation of the hydrogen bond contributed to the stabilization of the tertiary structure and increased thermostability of the mutant enzyme. If the postulation is the case, FGK thermostabilization would be possible similarly by the single amino acid substitution from Ser414 to another amino acid which could form the hydrogen bond with Ser329. We did a single amino acid substitution of the wild-type enzyme from Ser414 to Asn. As we expected, S414N showed comparable thermostability to that of S329D. On the other hand, a difference in kinetic properties for ATP between S414N and S329D was observed.

• 社団法人日本農芸化学会の論文
• 2002-06-23

著者

• OHSHIMA TOSHIHISA

  Department of Chemistry, Kyoto University of Education

• Sakuraba H

  Department Of Analytical Biochemistry Meiji Pharmaceutical University

• Takehara Hideki

  Molecular Gene Technics Genetic Resource Technology Kyushu University

• SAKASEGAWA SHIN-ICHI

  Diagnostics Division, Asahi Kasei Corporation

• MISAKI HIDEO

  Diagnostics Division, Asahi Kasei Corporation

• SAKURABA Haruhiko

  Department of Applied Biological Science, Faculty of Agriculture & Graduate School of Agriculture, K

• Misaki Hideo

  Diagnostics Division Asahi Kasei Corporation

• Misaki Hideo

  Asahi Chemical Industry Co. Ltd.

• YOSHIOKA Issei

  Asahi Chemical Industry

• YOSHIOKA Issei

  Diagnostics Research and Development Department, Asahi-Kasei Corporation

• Sakuraba Haruhiko

  Department Of Agricultural Chemistry University Of Osaka Prefecture

• Ohshima T

  Department Of Food Science And Technology Tokyo University Of Fisheries

• SAKASEGAWA Shin-ichi

  Asahi Kasei Corporation

• Yoshioka I

  Diagnostics Research And Development Department Asahi-kasei Corporation

• Ohshima T

  Microbial Genetics Division Institute Of Genetic Resources Faculty Of Agriculture Kyushu University

• Ohshima Toshihisa

  Department Of Biological Science And Technology Faculty Of Engineering The University Of Tokushima

• Sakasegawa Shin-ichi

  Diagnostics Division Asahi Kasei Corporation

• Misaki H

  Asahi Kasei Corporation

• Ohshima Toshihisa

  Microbial Genetics Division, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University

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