Introduction of an intramolecular crosslink at the active site of glyceraldehyde 3-phosphate dehydrogenase.
Introduction of an intramolecular crosslink at the active site of glyceraldehyde 3-phosphate dehydrogenase.
复制标题
在 3-磷酸甘油醛脱氢酶的活性位点引入分子内交联。
DOI：
10.1016/0006-291x(71)90627-9
复制
发表时间：
1971
影响因子：
3.1
通讯作者：
M. Tauber
中科院分区：
文献类型：
--
作者：
S. Shaltiel;M. Tauber
兔肌脱辅基甘油醛3 -磷酸脱氢酶与每摩尔酶原体1摩尔1，5-二氟，2，4-二硝基苯的反应导致酶活性的完全丧失，并伴随着在酶活性位点引入共价分子内交联。在消化酶消化后，一对交联的肽被纯化，并发现具有以下结构：交联的半胱氨酸和赖氨酸残基，尽管在一级序列中相隔约32个氨基酸残基，但在酶的三维结构中可以彼此接近5-6个氨基酸残基。
Reaction of rabbit muscle apo-glyceraldehyde 3 -phosphate dehydrogenase with one mole of 1, 5-difluoro, 2, 4-dinitrobenzene per mole of enzyme protomer brings about total loss of enzymatic activity and concomitant introduction of covalent intramolecular crosslinks at the active site of the enzyme. Following peptic digestion, a crosslinked couple of peptides was purified and found to have the structure: The crosslinked cysteine and lysine residues, though some 32 amino acid residues apart in the primary sequence, may approach each other to a distance of 5–6 Å in the three dimensional structure of the enzyme.