影响3-磷酸甘油醛脱氢酶中辅酶结合和亚基相互作用的因素

Factors affecting coenzyme binding and subunit interactions in glyceraldehyde-3-phosphate dehydrogenase.

作者信息

Reynolds C H, Dalziel K

出版信息

Biochim Biophys Acta. 1979 Apr 12;567(2):287-94. doi: 10.1016/0005-2744(79)90114-1.

Abstract

There is no evidence, at pH 9.4, of negative cooperativity in the binding of NAD+ or NADH to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phorphorylating), EC 1.2.1.12) nor in the binding of acetyl pyridine adenine dinucleotide at pH 7.6 and ph 9.4. The binding of NAD+ to carboxymethylated enzyme at pH 7.6 and pH 9.4 also occurs without cooperativity. The possible implications of these findings for the involvement of ionising groups in the enzyme in the subunit interactions responsible for negative cooperativity, previously reported for coenzyme binding at pH 7.4--8.6, are discussed.

摘要

在pH 9.4时，没有证据表明NAD⁺或NADH与兔肌甘油醛-3-磷酸脱氢酶（D-甘油醛-3-磷酸：NAD⁺氧化还原酶（磷酸化），EC 1.2.1.12）的结合存在负协同效应，在pH 7.6和pH 9.4时，乙酰吡啶腺嘌呤二核苷酸的结合也不存在负协同效应。在pH 7.6和pH 9.4时，NAD⁺与羧甲基化酶的结合也没有协同性。此前报道在pH 7.4 - 8.6时辅酶结合存在负协同效应，本文讨论了这些发现对于酶中电离基团参与负责负协同效应的亚基相互作用的可能意义。