组氨酸-298残基在链霉菌R61细胞外DD-肽酶催化机制中的重要性。
Importance of the His-298 residue in the catalytic mechanism of the Streptomyces R61 extracellular DD-peptidase.
作者信息
Hadonou A M, Jamin M, Adam M, Joris B, Dusart J, Ghuysen J M, Frère J M
机构信息
Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Belgium.
出版信息
Biochem J. 1992 Mar 1;282 ( Pt 2)(Pt 2):495-500. doi: 10.1042/bj2820495.
Abstract
Among the active-site-serine penicillin-recognizing proteins, the Streptomyces R61 extracellular DD-peptidase is the only one to have a His-Thr-Gly sequence [instead of Lys-Thr(Ser)-Gly] in 'box' VII. The His residue was replaced by Gln or Lys. Both mutations induced a marked decrease in the rates of both tripeptide substrate hydrolysis and acylation by benzylpenicillin and cephalosporin C. The rate of hydrolysis of the thioester hippuryl thioglycollate was less affected. The most striking result was the disproportionate loss of transpeptidation properties by both mutants, indicating an important role of His-298 in this reaction. We believe that this result represents the first modification of a DD-peptidase leading to a specific decrease of the transpeptidation-to-hydrolysis ratio.
摘要
在活性位点丝氨酸青霉素识别蛋白中，链霉菌R61细胞外DD - 肽酶是唯一在“框”VII中具有His - Thr - Gly序列[而非Lys - Thr(Ser) - Gly]的蛋白。His残基被Gln或Lys取代。两种突变均导致三肽底物水解速率以及苄青霉素和头孢菌素C酰化速率显著降低。硫酯马尿酸硫代乙醇酸酯的水解速率受影响较小。最显著的结果是两种突变体的转肽性质不成比例地丧失，表明His - 298在该反应中起重要作用。我们认为这一结果代表了DD - 肽酶的首次修饰，导致转肽与水解比率的特异性降低。
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