論文

査読有り
2002年7月

Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases

PROTEIN ENGINEERING
  • M Maeda
  • ,
  • H Kaku
  • ,
  • M Shimada
  • ,
  • T Nishioka

担当区分
筆頭著者, 責任著者
15
7
開始ページ
611
終了ページ
617
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/protein/15.7.611
出版者・発行元
OXFORD UNIV PRESS

Sequence analysis of a cDNA for D-erythrulose reductase from chicken liver showed that the deduced open reading frame encodes the protein with a molecular mass of 26 kDa consisting of 246 amino acids. Although the reductase shares more than 60% identity in the amino acid sequence with the mouse tetrameric carbonyl reductase, these two enzymes have many biochemical differences; their substrate specificity, subcellular localization, organ distribution, etc. A three-dimensional structure of D-erythrulose reductase was predicted by comparative modeling based on the structure of the tetrameric carbonyl reductase (PDB entry = 1CYD). Most of the residues at the active site (within 4 Angstrom from the ligand) of the carbonyl reductase were also conserved in the D-erythrulose reductase. Nevertheless, Val190 and Leu146 in the active site of the tetrameric carbonyl reductase were substituted in the D-erythrulose reductase by Asn192 and His148, respectively. The substitutions in the active sites may be related to the difference in substrate specificity of the two enzymes. The phylogenic analysis of D-erythrulose reductase and the other related proteins suggests that the protein described as a carbonyl reductase D-erythrulose reductase.

Web of Science ® 被引用回数 : 5

リンク情報
DOI
https://doi.org/10.1093/protein/15.7.611
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/12200544
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000177759200010&DestApp=WOS_CPL

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