DIRECT OBSERVATION OF SUBSTRATE DISTORTION BY TRIOSEPHOSPHATE ISOMERASE USING FOURIER-TRANSFORM INFRARED-SPECTROSCOPY
DIRECT OBSERVATION OF SUBSTRATE DISTORTION BY TRIOSEPHOSPHATE ISOMERASE USING FOURIER-TRANSFORM INFRARED-SPECTROSCOPY
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DOI：
10.1021/bi00544a012
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发表时间：
1980-01-01
期刊：
影响因子：
2.9
通讯作者：
KNOWLES, JR
中科院分区：
文献类型：
--
作者：
BELASCO, JG;KNOWLES, JR
测定了与[鸡肌肉]磷酸丙糖异构酶结合的磷酸二羟丙酮的红外光谱。有2个羰基带对应于结合底物，强度比约为3：1。相对于游离溶液中磷酸二羟丙酮的羰基吸收，主带移动了19 cm-1至1713 cm-1，提供了酶诱导底物畸变的直接证据。这种菌株可能是由于一种酶的亲电体，极化的底物的羰基，从而促进催化。
The IR spectrum of dihydroxyacetone phosphate bound to [chicken muscle] triose phosphate isomerase was measured. There are 2 carbonyl bands corresponding to the bound substrate, with an intensity ratio of about 3:1. Relative to the carbonyl absorption of dihydroxyacetone phosphate in free solution, the major band is shifted by 19 cm-1 to 1713 cm-1, providing direct evidence of enzyme-induced distortion of the substrate. This strain is probably attributable to an enzymic electrophile that polarizes the carbonyl group of the substrate and thereby promotes catalysis.