STEREOCHEMISTRY OF THE PEPTIDE ALPHA-AMIDATION REACTION INVOLVING 2 ENZYMES, PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) AND PEPTIDYLHYDROXYGLYCINE N-C LYASE (PHL)

被引：19

作者：

KAWAHARA, T

SUZUKI, K

IWASAKI, Y

SHIMOI, H

AKITA, M

MOROOKA, Y

NISHIKAWA, Y

机构：

[1] CIBA GEIGY JAPAN LTD,INT RES LABS,BIOORGAN RES DEPT,10-66 MIYUKICHO,TAKARAZUKA 665,JAPAN

[2] TOKYO INST TECHNOL,RESOURCES UTILIZAT RES LAB,MIDORI KU,YOKOHAMA,KANAGAWA 227,JAPAN

来源：

JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS | 1992年 / 08期

关键词：

D O I：

10.1039/c39920000625

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Peptidylglycine alpha-hydroxylating monooxygenase (PHM), the first enzyme involved in the peptide alpha-amidation, has been shown to convert N-benzoylglycine, a model substrate, stereoselectively to S-N-benzoyl-alpha-hydroxyglycine, whereas peptidylhydroxyglycine N-C lyase (PHL), the second enzyme, has been found to react exclusively with S-form of the intermediate.

引用

收藏

页码：625 / 626

页数：2

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