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2
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Biochemistry. 1996 Dec 17;35(50):16195-204. doi: 10.1021/bi961866d.
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Structure-guided engineering of the coenzyme specificity of Pseudomonas fluorescens mannitol 2-dehydrogenase to enable efficient utilization of NAD(H) and NADP(H).通过结构引导工程改造荧光假单胞菌甘露醇2-脱氢酶的辅酶特异性，以实现对NAD(H)和NADP(H)的高效利用。
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6
Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.荧光假单胞菌甘露醇脱氢酶中质子转移的动态机制：可移动的 GLU292 通过连接活性位点与主体溶剂的水通道来控制质子传递。
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On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase.论布朗斯特催化在荧光假单胞菌甘露醇2-脱氢酶中的作用
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本文引用的文献

1
Examining the relative timing of hydrogen abstraction steps during NAD(+)-dependent oxidation of secondary alcohols catalyzed by long-chain D-mannitol dehydrogenase from Pseudomonas fluorescens using pH and kinetic isotope effects.利用pH和动力学同位素效应，研究荧光假单胞菌长链D-甘露醇脱氢酶催化的仲醇NAD(+)依赖性氧化过程中氢提取步骤的相对时间。
Biochemistry. 2002 Aug 6;41(31):10158-65. doi: 10.1021/bi025517x.
2
Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.甘油脱氢酶。III族多元醇脱氢酶的结构、特异性及作用机制。
Structure. 2001 Sep;9(9):789-802. doi: 10.1016/s0969-2126(01)00645-1.
3
The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.双孢蘑菇中甘露醇2-脱氢酶NADP⁺二元复合物的晶体结构
J Biol Chem. 2001 Jul 20;276(29):27555-61. doi: 10.1074/jbc.M102850200. Epub 2001 May 2.
4
Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer.马肝乙醇脱氢酶柔性环中的取代作用阻碍构象变化并揭示氢转移。
Biochemistry. 1999 Oct 19;38(42):13951-9. doi: 10.1021/bi991731i.
5
Kinetic study of the catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens.荧光假单胞菌甘露醇脱氢酶催化机制的动力学研究
Biochemistry. 1999 Aug 10;38(32):10489-98. doi: 10.1021/bi990327g.
6
The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution.分辨率为1.9埃的黎巴嫩果蝇乙醇脱氢酶的精细晶体结构。
J Mol Biol. 1998 Sep 18;282(2):383-99. doi: 10.1006/jmbi.1998.2015.
7
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.空位BLAST和位置特异性迭代BLAST：新一代蛋白质数据库搜索程序。
Nucleic Acids Res. 1997 Sep 1;25(17):3389-402. doi: 10.1093/nar/25.17.3389.
8
Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodobacter sphaeroides.球形红杆菌甘露醇脱氢酶基因的克隆、核苷酸序列及特性分析
J Gen Microbiol. 1993 Oct;139(10):2475-84. doi: 10.1099/00221287-139-10-2475.
9
A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins.中链脱氢酶/还原酶（MDR）超家族。亚系包括ζ-晶状体蛋白、醇脱氢酶和多元醇脱氢酶、醌氧化还原酶烯酰还原酶、VAT-1及其他蛋白质。
Eur J Biochem. 1994 Nov 15;226(1):15-22. doi: 10.1111/j.1432-1033.1994.tb20021.x.
10
Short-chain dehydrogenases/reductases (SDR).短链脱氢酶/还原酶（SDR）
Biochemistry. 1995 May 9;34(18):6003-13. doi: 10.1021/bi00018a001.

荧光假单胞菌D-甘露醇2-脱氢酶（一种多元醇特异性长链脱氢酶家族成员）的催化共有基序，通过对该酶定点突变体的动力学表征揭示。

A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens.

作者信息

Klimacek Mario, Nidetzky Bernd

机构信息

Institute of Biotechnology, Graz University of Technology, Petersgasse 12/I, A-8010 Graz, Austria.

出版信息

Biochem J. 2002 Oct 1;367(Pt 1):13-8. doi: 10.1042/BJ20020932.

DOI:10.1042/BJ20020932
PMID:12175334
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1222881/
Abstract

Lys-295, Asn-300 and His-303 of D-mannitol 2-dehydrogenase from Pseudomonas fluorescens were mutated individually into alanine (K295A, N300A and H303A respectively). Purified mutants displayed catalytic efficiencies for NAD(+)-dependent oxidation of D-mannitol 300-fold (H303A), 1000-fold (N300A) and approx. 400000-fold (K295A) below the wild-type level. Comparison of primary kinetic isotope effects on kinetic parameters for D-fructose reduction by wild-type and mutants at pH 10.0 demonstrate that Asn-300 has an auxiliary role in stabilization of the transition state of hydride transfer, and His-303 contributes to substrate positioning. The large solvent isotope effect of 11+/-1 on k (cat) for mannitol oxidation by K295A at pH((2)H) 10.5 suggests a role for Lys-295 in general base enzymic catalysis. Positional conservation of Lys-295, Asn-300 and His-303 across a family of polyol-specific long-chain dehydrogenases suggests a unique catalytic signature: Lys-Xaa(4)-Asn-Xaa(2)-His (where 'Xaa' denotes 'any amino acid').

摘要

荧光假单胞菌D-甘露醇2-脱氢酶的赖氨酸-295、天冬酰胺-300和组氨酸-303分别被单独突变为丙氨酸（分别为K295A、N300A和H303A）。纯化后的突变体对D-甘露醇的NAD(+)依赖性氧化的催化效率比野生型水平低300倍（H303A）、1000倍（N300A）和约400000倍（K295A）。对野生型和突变体在pH 10.0条件下D-果糖还原动力学参数的一级动力学同位素效应进行比较，结果表明，天冬酰胺-300在稳定氢化物转移过渡态方面具有辅助作用，而组氨酸-303有助于底物定位。K295A在pH((2)H) 10.5条件下对甘露醇氧化的k (cat)具有11±1的大溶剂同位素效应，这表明赖氨酸-295在一般碱催化中发挥作用。赖氨酸-295、天冬酰胺-300和组氨酸-303在一族多元醇特异性长链脱氢酶中的位置保守性表明了一种独特的催化特征：赖氨酸-Xaa(4)-天冬酰胺-Xaa(2)-组氨酸（其中“Xaa”表示“任何氨基酸”）。