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
Biochemistryjournal_title
Biochemistryauthors
Butler-Ransohoff JE,Kendall DA,Freeman S,Knowles JR,Kaiser ETdoi
10.1021/bi00413a029subject
Has Abstractpub_date
1988-06-28 00:00:00pages
4777-80issue
13eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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