Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase.

Abstract:

:The stereochemical course of the phospho group transfer catalyzed by mutant (S102C) alkaline phosphatase from Escherichia coli was investigated by using 31P nuclear magnetic resonance spectroscopy. Transphosphorylation from 4-nitrophenyl (Rp)-[16O, 17O, 18O]phosphate to (S)-propane-1,2-diol occurs with overall retention of configuration at phosphorus. This result is consistent with the view that the hydrolysis of substrates by this mutant enzyme proceeds by way of a covalent phosphoenzyme intermediate in the same manner as the wild-type alkaline phosphatase.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Butler-Ransohoff JE,Kendall DA,Freeman S,Knowles JR,Kaiser ET

doi

10.1021/bi00413a029

subject

Has Abstract

pub_date

1988-06-28 00:00:00

pages

4777-80

issue

13

eissn

0006-2960

issn

1520-4995

journal_volume

27

pub_type

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