2002年6月
Stabilization of Flavobacterium meningosepticum glycerol kinase by introduction of a hydrogen bond
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
- ,
- ,
- ,
- ,
- ,
- 巻
- 66
- 号
- 6
- 開始ページ
- 1374
- 終了ページ
- 1377
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1271/bbb.66.1374
- 出版者・発行元
- TAYLOR & FRANCIS LTD
The thermostability of Havobacterium 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.
- リンク情報
- ID情報
-
- DOI : 10.1271/bbb.66.1374
- ISSN : 0916-8451
- eISSN : 1347-6947
- PubMed ID : 12162561
- Web of Science ID : WOS:000176603800025