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Volumn 39, Issue 31, 2000, Pages 9451-9458

Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases

(4) Holtz, K M a Catrina, I E b Hengge, A C b Kantrowitz, E R a

a BOSTON COLLEGE (United States)

b UTAH STATE UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; ALKALINE PHOSPHATASE; ARGININE; PHOSPHORUS; PHOSPHORUS ACID DERIVATIVE; THIOL GROUP;

ARTICLE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME MODIFICATION; HYDROLYSIS; MUTATION; PRIORITY JOURNAL; REACTION ANALYSIS;

ALANINE; ALKALINE PHOSPHATASE; ARGININE; ENZYME INHIBITORS; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; LINEAR ENERGY TRANSFER; MUTAGENESIS, SITE-DIRECTED; NITROPHENOLS; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHATES; SUBSTRATE SPECIFICITY; THIONUCLEOTIDES;

EID: 0034622591 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000899x Document Type: Article

Times cited : (41)

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