Kim H J, Balcezak T J, Nathin S J, McMullen H F, Hansen D E
Department of Chemistry, Amherst College, Massachusetts 01002.
Anal Biochem. 1992 Nov 15;207(1):68-72. doi: 10.1016/0003-2697(92)90501-w.
We have developed a continuous spectrophotometric assay for S-adenosylmethionine synthetase and, using this assay, have examined the interaction of five potential inhibitors with the E. coli enzyme. S-Vinylhomocysteine and S-allylhomocysteine were found to be substrates, while S-(methanethio)cysteine and S-(methanethio)homocysteine were found to be competitive inhibitors. S-Cyanohomocysteine is neither a substrate nor an inhibitor.
我们开发了一种用于S-腺苷甲硫氨酸合成酶的连续分光光度测定法,并使用该测定法研究了五种潜在抑制剂与大肠杆菌酶的相互作用。发现S-乙烯基高半胱氨酸和S-烯丙基高半胱氨酸是底物,而S-(甲硫基)半胱氨酸和S-(甲硫基)高半胱氨酸是竞争性抑制剂。S-氰基高半胱氨酸既不是底物也不是抑制剂。