胃蛋白酶催化的氨基转肽反应机制。
Mechanism of pepsin-catalyzed aminotranspeptidation reactions.
作者信息
Balbaa M, Blum M, Hofmann T
机构信息
Department of Biochemistry, Faculty of Science, Alexandria University, Egypt.
出版信息
Int J Biochem. 1994 Jan;26(1):35-42. doi: 10.1016/0020-711x(94)90192-9.
PMID:8138045
Abstract
- The tetrapeptide Ala2-Nph2 (where Nph = p-nitrophenylalanyl) is treated by porcine pepsin to study the mechanism of aminotranspeptidation reactions. 2. The major initial product is Ala2-Nph and the major transpeptidation products are Nph2 and Nph3 accompanied by some Nph, a little Nph4, Ala2-Nph3 and Ala2-Nph4. 3. Oligomers of Nph greater than tetramers are formed near the end of the reaction. 4. In presence of [3H]Nph, no incorporation of Nph into the transpeptidation products is observed. 5. 18O-labeling shows extensive incorporation of 18O atoms from [18O]water in the carbonyl oxygens of Nph residues.
摘要
- 用猪胃蛋白酶处理四肽Ala2-Nph2（其中Nph = 对硝基苯丙氨酰基）以研究氨转移肽反应的机制。2. 主要的初始产物是Ala2-Nph，主要的转肽产物是Nph2和Nph3，伴有一些Nph、少量Nph4、Ala2-Nph3和Ala2-Nph4。3. 在反应接近尾声时形成了大于四聚体的Nph低聚物。4. 在[3H]Nph存在的情况下，未观察到Nph掺入转肽产物中。5. 18O标记显示来自[18O]水的18O原子大量掺入Nph残基的羰基氧中。
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