Raine A R, Yang C C, Packman L C, White S A, Mathews F S, Scrutton N S
Department of Biochemistry, University of Cambridge, United Kingdom.
Protein Sci. 1995 Dec;4(12):2625-8. doi: 10.1002/pro.5560041222.
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.
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。