An investigation of the active site of lactate dehydrogenase with NAD+ analogues.
An investigation of the active site of lactate dehydrogenase with NAD+ analogues.
复制标题
用 NAD 类似物研究乳酸脱氢酶的活性位点。
DOI：
10.1111/j.1432-1033.1981.tb05737.x
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Rossmann,MG
中科院分区：
文献类型：
--
作者：
Samama,JP;Marchal-Rosenheimer,N;Biellmann,JF;Rossmann,MG
研究了18种NAD+类似物对角鲨M4、兔M4和牛肉h4乳酸脱氢酶的动力学性质，并对烟酰胺部分进行了改变。存在于吡啶C‐3上的基团的大小可以在不损失辅酶活性的情况下大量增加。试验组为硫胺、甲基、乙基、重氮酮和氯乙酰。位置C‐4和C‐5的取代阻止了氢化物转移的正确定位，并可能阻碍与酶的结合。吡啶-腺嘌呤二核苷酸及其3 -碘衍生物的动力学性质揭示了酰胺在C - 3上的结合作用，而3 -氰吡啶-腺嘌呤二核苷酸是一种强抑制剂。
The kinetic properties of 18 NAD+analogues, with alterations to the nicotinamide moiety, have been studied with respect to dogfish M4, rabbit M4and beef H4lactate dehydrogenases.The size of the groups present at C‐3 of the pyridinium can be increased quite extensively without loss of coenzyme activity. Groups tested were thioamide, methyl, ethyl, diazoketone and chloroacetyl.Substitutions at positions C‐4 and C‐5 prevent proper positioning for hydride transfer and can hinder binding to the enzyme. The kinetic properties of pyridine‐adenine dinucleotide and its 3‐iodo derivative reveal the bidning role of the amide at C‐3 whereas 3‐cyanopyridine‐adenine dinculeotide is a strong inhibitor.