Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase

Journal Article · Tue Jun 28 00:00:00 EDT 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00413a029· OSTI ID:6804287

Butler-Ransohoff, J E; Kendall, D A; Freeman, S; Knowles, J R; Kaiser, E T

The stereochemical course of the phospho group transfer catalyzed by mutant (S102C) alkaline phosphatase from Escherichia coli was investigated by using /sup 31/P nuclear magnetic resonance spectroscopy. Transphosphorylation from 4-nitrophenyl (R/sub P/)-/sup 17/O, /sup 16/O, /sup 18/O)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.

• Research Organization: Rockefeller Univ., New York, NY (USA)
• OSTI ID: 6804287
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:13; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ALKALINE PHOSPHATASE
BACTERIA
ENZYMES
ESCHERICHIA COLI
ESTERASES
EVEN-EVEN NUCLEI
EVEN-ODD NUCLEI
HYDROLASES
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
NITRO COMPOUNDS
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXYGEN 16
OXYGEN 17
OXYGEN 18
OXYGEN ISOTOPES
PHOSPHATASES
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
RESONANCE
STABLE ISOTOPES
STEREOCHEMISTRY