Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.
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Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal IonCellular function and molecular structure of ecto-nucleotidases.Function assignment to conserved residues in mammalian alkaline phosphatases.Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site.All-enzymatic HPLC method for determination of individual and total contents of vitamin B(6) in foods.Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties.Effects of replacing active site residues in a cold-active alkaline phosphatase with those found in its mesophilic counterpart from Escherichia coli.
P2860
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P2860
Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
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name
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@en
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@nl
type
label
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@en
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@nl
prefLabel
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@en
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@nl
P356
P1433
P1476
Binding of magnesium in a muta ...... tep in the reaction mechanism.
@en
P2093
P304
10683-10691
P356
10.1021/BI00091A019
P407
P577
1993-10-01T00:00:00Z