磷酸丙糖异构酶的活性中心。
The active centre of triose phosphate isomerase.
作者信息
Burton P M, Waley S G
出版信息
Biochem J. 1966 Sep;100(3):702-10. doi: 10.1042/bj1000702.
Abstract
The molecular weight and amino acid composition of triose phosphate isomerase have been determined. The molecular weight (43000) is lower and the molecular activity (500000) higher than those of most other glycolytic enzymes. Reaction with iodoacetate (studied with radioactive reagent) takes place in two phases: in the first phase, at pH6.3, cysteine and methionine groups react and enzymic activity is unimpaired; in the second phase, histidine reacts and enzymic activity is lost. Photo-oxidation leads to inactivation, with loss of cysteine, of histidine and of tryptophan, but little loss of tyrosine. The mechanism postulated for the action of the enzyme demands the intervention of a group functioning as a base, and the results obtained are consistent with histidine's being the basic group in the active centre.
摘要
磷酸丙糖异构酶的分子量和氨基酸组成已被测定。其分子量（43000）低于大多数其他糖酵解酶，分子活性（500000）则高于它们。与碘乙酸的反应（用放射性试剂研究）分两个阶段进行：在第一阶段，在pH6.3时，半胱氨酸和甲硫氨酸基团发生反应，酶活性不受影响；在第二阶段，组氨酸发生反应，酶活性丧失。光氧化导致酶失活，同时半胱氨酸、组氨酸和色氨酸损失，但酪氨酸损失很少。该酶作用所假定的机制需要一个起碱作用的基团参与，所获得的结果与组氨酸是活性中心的碱性基团这一观点一致。
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