Arg-94 is crucial to the catalysis of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8

被引：4

作者：

Fujita, M ^{[1
]}

Toyooka, Y ^{[1
]}

Tamegai, H ^{[1
]}

Eguchi, T ^{[1
]}

Kakinuma, K ^{[1
]}

机构：

[1] Tokyo Inst Technol, Dept Chem, Meguro Ku, Tokyo 1528551, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 9卷 / 4-6期

关键词：

Thermus thermophilus HB-8; 3-isopropylmalate dehydrogenase; site-directed mutagenesis; catalytic residue;

D O I：

10.1016/S1381-1177(99)00091-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crucial role of Arg-94 in 3-isopropylmalate (IPM) dehydrogenase from Thermus thermophilus HB8 was elucidated by replacing the residue to lysine with site-directed mutagenesis. The k(cat) value of the R94K mutant enzyme for IPM was significantly reduced to 1/170 compared with that of native enzyme, whereas the K-m for IPM was not much changed. It appeared that the major role of Arg-94 in exerting the enzymatic activity is not for the substrate recognition, but for the reaction catalysis, in such a way that Arg-94 facilitates stabilization of the transition-state in the decarboxylation step. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：149 / 155

页数：7

共 50 条

[21] Production of polyhydroxyalkanoates from whey by Thermus thermophilus HB8
Pantazaki, Anastasia A.
Papaneophytou, Christos P.
Pritsa, Agathi G.
Liakopoulou-Kyriakides, Maria
Kyriakidis, Dimitrios A.
PROCESS BIOCHEMISTRY, 2009, 44 (08) : 847 - 853
[22] Synthesis of conformationally restricted substrate analogs and their interaction with 3-isopropylmalate dehydrogenase derived from Thermus thermophilus
Chiba, A
Eguchi, T
Oshima, T
Kakinuma, K
TETRAHEDRON, 1997, 53 (10) : 3537 - 3544
[23] CRYSTAL STRUCTURE OF ACYL-CoA DEHYDROGENASE OF THERMUS THERMOPHILUS HB8
Hamada, K.
Ago, H.
Sugahara, M.
Nishio, K.
Nodake, Y.
Miyano, M.
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2002, 58 : C300 - C300
[24] A DNA METHYLASE FROM THERMUS-THERMOPHILUS HB8
SATO, S
NAKAZAWA, K
SHINOMIYA, T
JOURNAL OF BIOCHEMISTRY, 1980, 88 (03): : 737 - 747
[25] Analysis of the effect of accumulation of amino acid replacements on activity of 3-isopropylmalate dehydrogenase from Thermus thermophilus
Yasugi, M
Suzuki, T
Yamagishi, A
Oshima, T
PROTEIN ENGINEERING, 2001, 14 (08): : 601 - 607
[26] STEREOCHEMISTRY OF THE DECARBOXYLATION REACTION CATALYZED BY 3-ISOPROPYLMALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS-THERMOPHILUS
KAKINUMA, K
OZAWA, K
FUJIMOTO, Y
AKUTSU, N
OSHIMA, T
JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS, 1989, (17) : 1190 - 1192
[27] High thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus resulting from low ΔCp of unfolding
Motono, C
Oshima, T
Yamagishi, A
PROTEIN ENGINEERING, 2001, 14 (12): : 961 - 966
[28] Atomic level description of the domain closure in a dimeric enzyme: Thermus thermophilus 3-isopropylmalate dehydrogenase
Graczer, Eva
Merli, Angelo
Singh, Rajesh Kumar
Karuppasamy, Manikandan
Zavodszky, Peter
Weiss, Manfred S.
Vas, Maria
MOLECULAR BIOSYSTEMS, 2011, 7 (05) : 1646 - 1659
[29] CRYSTALLIZATION AND PRELIMINARY-X-RAY DATA FOR 3-ISOPROPYLMALATE DEHYDROGENASE OF THERMUS-THERMOPHILUS
KATSUBE, Y
TANAKA, N
TAKENAKA, A
YAMADA, T
OSHIMA, T
JOURNAL OF BIOCHEMISTRY, 1988, 104 (05): : 679 - 680
[30] TYR-139 IN THERMUS-THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE IS INVOLVED IN CATALYTIC FUNCTION
MIYAZAKI, K
OSHIMA, T
FEBS LETTERS, 1993, 332 (1-2) : 37 - 38

← 1 2 3 4 5 →