The role of residues Arg169 and Arg220 in intersubunit interactions of yeast D-amino acid oxidase

被引：3

作者：

Cherskova, N. V. ^{[1
,2
]}

Khoronenkova, S. V. ^{[1
,3
]}

Tishkov, V. I. ^{[1
,2
]}

机构：

[1] Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119992, Russia

[2] Russian Acad Sci, AN Bach Inst Biochem, Moscow 117234, Russia

[3] Innovat & High Technol MSU Ltd, Moscow 109559, Russia

来源：

RUSSIAN CHEMICAL BULLETIN | 2010年 / 59卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

D-amino acid oxidase; site-directed mutagenesis; quaternary structure; substrate specificity; thermal stability; RHODOTORULA-GRACILIS; CRYSTAL-STRUCTURE; RESOLUTION; MECHANISM; STATE; FORM;

D O I：

10.1007/s11172-010-0072-9

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

D-Amino acid oxidase from the yeast Trigonopsis variabilis (EC 1.4.3.3, TvDAAO) exists as a dimer consisting of two identical subunits. The dimeric structure of the enzyme is stabilized by 12 (six pairs) hydrogen bonds, the residues Arg169 and Arg220 of each subunit being involved in eight hydrogen bonds. The Arg169Glu and Arg(169,220)Ala mutants of TvDAAO were prepared. Both mutant enzymes were expressed in E. coli cells as insoluble but catalytically active inclusion bodies. The introduction of amino acid substitutions at the intersubunit interface resulted in a change in the substrate specificity profile and a strong decrease in thermal stability.

引用

页码：269 / 275

页数：7

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