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Literature summary for 3.1.3.1 extracted from

  • Holtz, K.M.; Kantrowitz, E.R.
    The mechanism of the alkaline phosphatase reaction: insight from NMR, crystallography and site-specific mutagenesis (1999), FEBS Lett., 462, 7-11.
    View publication on PubMed
Search for more literature for 3.1.3.1

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the covalent phospho-enzyme intermediate of the H331Q mutant enzyme and of the transition state complex between the wild-type enzyme and vanadate Escherichia coli

Protein Variants

Protein Variants Comment Organism
D101S weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 35fold higher activity Escherichia coli
D153G weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 5fold higher activity, reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium Escherichia coli
D153H reduced magnesium affinity, maximual activity is only achieved with the addition of exogenous magnesium Escherichia coli
D153H/K328A reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium Escherichia coli
K328A lower phosphate affinity, alteration in the rate-limiting step Escherichia coli
K328C lower phosphate affinity, alteration in the rate-limiting step Escherichia coli
K328H lower phosphate affinity, alteration in the rate-limiting step Escherichia coli
R166A mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold Escherichia coli
R166Q mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold Escherichia coli
R166S mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold Escherichia coli
S102A activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction,1000-10000fold reduction in the turnover number Escherichia coli
S102C activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 100fold reduction in turnover number Escherichia coli
S102G activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number Escherichia coli
S102L activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number Escherichia coli

General Stability

General Stability Organism
plays an indirect but important role in stabilizing the enzyme in its most active conformations Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00634
-
-

Reaction

Reaction Comment Organism Reaction ID
a phosphate monoester + H2O = an alcohol + phosphate double in-line displacement mechanism involving two-metal ion catalysis Escherichia coli
a