大肠杆菌β-胱硫醚酶的磷酸吡哆醛5'-磷酸结合位点与胱硫醚γ-合酶的序列比较
Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences.
作者信息
Martel A, Bouthier de la Tour C, Le Goffic F
出版信息
Biochem Biophys Res Commun. 1987 Sep 15;147(2):565-71. doi: 10.1016/0006-291x(87)90968-5.
The phosphopyridoxyl peptides of beta cystathionase and cystathionine gamma synthase of Escherichia Coli were identified after reduction, carboxymethylation and proteolysis of the holoenzymes. Their comparison with those obtained from rat liver gamma cystathionase (Fearon, C.W., Rodkey, J.A. and Abeles R.H. 1982. Biochemistry 21 3790-3794.) showed a high degree of homology between the three PLP binding sites with the presence of the tripeptide sequence: Thr-Lys(Pxy)-Tyr in their structure. This homology suggests that these enzymes of methionine metabolism have probably the same origin.
在对大肠杆菌的β-胱硫醚酶和胱硫醚γ-合酶的全酶进行还原、羧甲基化和蛋白水解后，鉴定出了它们的磷酸吡哆醛肽。将其与从大鼠肝脏γ-胱硫醚酶获得的肽段进行比较（费伦，C.W.，罗德基，J.A.和阿贝莱斯，R.H. 1982年。《生物化学》21卷，3790 - 3794页），结果表明这三种磷酸吡哆醛结合位点之间具有高度同源性，其结构中存在三肽序列：苏氨酸-赖氨酸（磷酸吡哆醛化）-酪氨酸。这种同源性表明，这些甲硫氨酸代谢酶可能有着相同的起源。
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