STEREOSPECIFIC LYSIS OF A RANGE OF BETA-HYDROXY-ALPHA-AMINO ACIDS CATALYZED BY A NOVEL ALDOLASE FROM STREPTOMYCES-AMAKUSAENSIS

被引：31

作者：

HERBERT, RB ^{[1
]}

WILKINSON, B ^{[1
]}

ELLAMES, GJ ^{[1
]}

KUNEC, EK ^{[1
]}

机构：

[1] STERLING WINTHROP PHARMACEUT RES DIV,STERLING WINTHROP RES CTR,DEPT CHEM DEV,ALNWICK NE66 2JH,NORTHD,ENGLAND

来源：

JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS | 1993年 / 02期

关键词：

D O I：

10.1039/c39930000205

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Cell-free preparations of Streptomyces amakusaensis contain a novel aldolase which catalyses the conversion of beta-hydroxy-alpha-amino acids (as 2) into the corresponding aldehyde plus glycine; the aldolase is stable, shows broad substrate tolerance, is highly selective for threo stereochemistry and, where examined, is stereospecific for the (2S,3R) configuration.

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页码：205 / 206

页数：2

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