论文部分内容阅读
D甘油醛-3-磷酸脱氢酶(D-glyceraldehyde-3-phesphate-dehydrogenase,GAPDH)是一个重要的别构酶。对肌肉来源的GAPDH活性中心的羧甲基化是全位的,而生成新荧光物质的反应是半位的。这可能表现了GAPDH 4个亚基的协同性。前文已经报道了2.7分辨率带NAD~+荧光衍生物GAPDH(简称光照酶)的晶体结构,看到了结构的不对称性。
D-glyceraldehyde-3-phesphate-dehydrogenase (GAPDH) is an important allosteric enzyme. Carboxymethylation of the muscle-derived GAPDH active site is all-enviromental, whereas the reaction to create a new fluorescent substance is half-site. This may indicate the synergy of the four subunits of GAPDH. The crystal structure of GAPDH with NAD ~ + fluorescence derivative at 2.7 resolution has been previously reported and the structural asymmetry is seen.