CORRELATION OF COFACTOR BINDING AND THE QUATERNARY STRUCTURE OF PYRUVATE DECARBOXYLASE AS REVEALED BY P-31 NMR-SPECTROSCOPY

被引:10
|
作者
HUBNER, G [1 ]
KONIG, S [1 ]
SCHNACKERZ, KD [1 ]
机构
[1] UNIV WURZBURG,THEODOR BOVERI INST BIOWISSENSCH,W-8700 WURZBURG,GERMANY
关键词
PYRUVATE DECARBOXYLASE; THIAMINE PYROPHOSPHATE; P-31 NMR SPECTROSCOPY;
D O I
10.1016/0014-5793(92)81471-W
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The pH dependence of the quaternary structure of pyruvate decarboxylase (EC 4.1.1.1) has recently been discovered [(1990) FEBS Lett. 266, 17-20; (1992) Biochemistry (in press)]. In the present study we have investigated the change in quaternary structure by observing the binding of the cofactor, thiamine pyrophosphate, using P-31 NMR spectroscopy. The dissociation of the native tetramers into dimers when increasing the pH coincides with a weaker binding of the cofactor and loss of enzyme activity. The results provide further evidence that thiamine pyrophosphate is bound primarily via the beta-phosphate moiety. In addition, a phosphoserine has been discovered in two of the four subunits.
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页码:101 / 103
页数:3
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