ON THE ROLE OF GLU-68 IN ALCOHOL-DEHYDROGENASE

被引：84

作者：

RYDE, U

机构：

[1] Department of Theoretical Chemistry, University of Lund, Chemical Centre, Lund, S-221 00

来源：

PROTEIN SCIENCE | 1995年 / 4卷 / 06期

关键词：

COMBINED AB-INITIO AND MOLECULAR MECHANICAL GEOMETRY OPTIMIZATION 5-COORDINATION; GEOMETRY IMPOSED BY ENZYME; LIGAND EXCHANGE; MOLECULAR DYNAMICS; REACTION MECHANISM;

D O I：

10.1002/pro.5560040611

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：

Theoretical computations (molecular dynamics and combined quantum chemical and molecular mechanical geometry optimizations) have been performed on horse liver alcohol dehydrogenase. The results provide evidence that Glu-68, a highly conserved residue located 0.47 nm from the catalytic zinc ion, may intermittently coordinate to the zinc ion. Structures with Glu-68 coordinated to the zinc ion are almost as stable as structures with Glu-68 at the crystal position and the barrier between the two configurations of Glu-68 is so low that it can readily be bypassed at room temperature. There is a cavity behind the zinc ion that seems to be tailored to allow such coordination of Glu-68 to the zinc ion. It is suggested that Glu-68 may facilitate the exchange of ligands in the substrate site by coordinating to the zinc ion when the old ligand dissociates.

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收藏

页码：1124 / 1132

页数：9

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[21] Enhancing temperature resistance of polymer gel fracturing fluids: The role of alcohol [J].

Zhao, Mingwei ;

Yang, Ziteng ;

Meng, Xiangjuan ;

Xu, Zhongzheng ;

Wu, Yining ;

Dai, Caili .

GEOENERGY SCIENCE AND ENGINEERING, 2024, 242

[22] Efficient preparation of the chiral intermediate of luliconazole with Lactobacillus kefir alcohol dehydrogenase through rational rearrangement of the substrate binding pocket [J].

Zheng, Chenni ;

Wang, Zhiguo ;

Wang, Qian ;

Wang, Shenyong ;

Lao, Shuhua ;

He, Jin ;

Chen, Zhenming .

MOLECULAR CATALYSIS, 2021, 509

[23] Do Dynamic Effects Play a Significant Role in Enzymatic Catalysis? A Theoretical Analysis of Formate Dehydrogenase [J].

Roca, Maite ;

Oliva, Monica ;

Castillo, Raquel ;

Moliner, Vicente ;

Tunon, Inaki .

CHEMISTRY-A EUROPEAN JOURNAL, 2010, 16 (37) :11399-11411

[24] Conformational Dynamics-Guided Loop Engineering of an Alcohol Dehydrogenase: Capture, Turnover and Enantioselective Transformation of Difficult-to-Reduce Ketones [J].

Liu, Beibei ;

Qu, Ge ;

Li, Jun-Kuan ;

Fan, Wenchao ;

Ma, Jun-An ;

Xu, Yan ;

Nie, Yao ;

Sun, Zhoutong .

ADVANCED SYNTHESIS & CATALYSIS, 2019, 361 (13) :3182-3190

[25] Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways [J].

Hermann, Johannes ;

Nowotny, Phillip ;

Schrader, Tobias E. ;

Biggel, Philipp ;

Hekmat, Dariusch ;

Weuster-Botz, Dirk .

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2018, 74 :754-764

[26] Medium- and short-chain dehydrogenase/reductase gene and protein familiesStructure-function relationships in short-chain alcohol dehydrogenases [J].

R. Ladenstein ;

J.-O. Winberg ;

J. Benach .

Cellular and Molecular Life Sciences, 2008, 65

[27] The role of conformation states in the heterogeneity of fluorescence decay times in FAD in water-alcohol mixtures [J].

Volkov, Denis A. ;

Gorbunova, Ioanna A. ;

Yashkov, Dmitrii, V ;

Sasin, Maxim E. ;

Khrenova, Maria G. ;

Vasyutinskii, Oleg S. .

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY, 2025, 461

[28] Alcohol dehydrogenase: molecular dynamics study of conformational and orientational behaviour of the enzyme in complex with nad during sorption on the surface of electrode materials using graphite as an example [J].

Baigunov, Ivan A. ;

Kholmurodov, Kholmirzo T. ;

Gladyshev, Pavel P. .

NANOSYSTEMS-PHYSICS CHEMISTRY MATHEMATICS, 2025, 16 (02) :192-198

[29] Activation/Inactivation Role of Ionic Liquids on Formate Dehydrogenase from Pseudomonas sp 101 and Its Mutated Thermostable Form [J].

D'Oronzo, Erica ;

Secundo, Francesco ;

Minofar, Babak ;

Kulik, Natallia ;

Pometun, Anastasia A. ;

Tishkov, Vladimir I. .

CHEMCATCHEM, 2018, 10 (15) :3247-3259

[30] Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure [J].

Graczer, Eva ;

Szimler, Tamas ;

Garamszegi, Anita ;

Konarev, Petr V. ;

Labas, Aniko ;

Olah, Julianna ;

Pallo, Anna ;

Svergun, Dmitri I. ;

Merli, Angelo ;

Zavodszky, Peter ;

Weiss, Manfred S. ;

Vast, Maria .

BIOCHEMISTRY, 2016, 55 (03) :560-574

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