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2
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引用本文的文献

1
Crystal structure of histamine dehydrogenase from Nocardioides simplex.来自简单诺卡氏菌的组胺脱氢酶的晶体结构。
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Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.研究PC-PLC(Bc)蛋白变体底物特异性谱的结构研究。
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Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex.三甲胺脱氢酶H172Q突变体的还原半反应：反对碳负离子机制的证据以及酶-底物复合物中动力学影响电离的归属
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5
Cation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.阳离子-π键合及取代铵配体在生物分子识别中的氨基-芳香族相互作用
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6
Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine.野生型三甲胺脱氢酶及不同电荷突变酶中的黄素化作用：对黄素异咯嗪N1周围蛋白质环境的研究
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The reaction of trimethylamine dehydrogenase with diethylmethylamine.三甲胺脱氢酶与二乙甲基胺的反应。
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Electron tunneling in substrate-reduced trimethylamine dehydrogenase: kinetics of electron transfer and analysis of the tunneling pathway.
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Structural basis of antibody function.抗体功能的结构基础。
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Hydrogen bonding in globular proteins.球状蛋白质中的氢键。
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Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution.
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Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.加州电鳐乙酰胆碱酯酶的原子结构：一种典型的乙酰胆碱结合蛋白。
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利用侧链芳烃对铵阳离子进行蛋白质识别：仲铵配体的结构变异

Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.

作者信息

Raine A R, Yang C C, Packman L C, White S A, Mathews F S, Scrutton N S

机构信息

Department of Biochemistry, University of Cambridge, United Kingdom.

出版信息

Protein Sci. 1995 Dec;4(12):2625-8. doi: 10.1002/pro.5560041222.

DOI:10.1002/pro.5560041222
PMID:8580856
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143047/
Abstract

A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-pi bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-pi and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.

摘要

利用三甲胺脱氢酶的晶体坐标生成了二甲胺脱氢酶的结构模型。底物在三甲胺脱氢酶中通过阳离子-π键结合，但二甲胺脱氢酶的模型表明仲胺是通过阳离子-π键和传统氢键的混合方式结合的。在二甲胺脱氢酶中，结合在方向上更具特异性，且与那些结合叔胺和季胺基团的蛋白质不同。