Further evidence for oxygen exchange at an intermediate stage in myosin hydrolysis.
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Humans↗
Biomedical subjects
D E KOSHLAND
Publications and source records attributed to D E KOSHLAND.
Identification of amino acids involved in phosphoglucomutase action.
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Amino Acids↗
Cleavage point during hydrolyses catalyzed by ribonuclease and phosphodiesterase.
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Cytokinesis↗
A method for characterizing the type and numbers of groups involved in enzyme action.
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Enzymes↗
The active site and enzyme action.
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Catalytic Domain↗
Comparative structural studies of phosphoglucomutase and chymotrypsin.
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Chymotrypsin↗
Properties of the active site in myosin hydrolysis of adenosine triphosphate as indicated by the O18-exchange reaction.
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Adenine Nucleotides↗
Stereochemistry of enzyme, substrate, and products during beta-amylase action.
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Amylases↗
Enzyme flexibility and enzyme action.
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Enzymes↗
A mechanism for the effects of dinitrophenol and temperature on the hydrolytic activity of myosin.
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Dinitrophenols↗
Mechanism of hydrolysis of adenosinetriphosphate by muscle proteins and its relation to muscular contraction.
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Adenosine Triphosphate↗
The hydrolytic activity of glyceraldehyde-3-phosphate dehydrogenase.
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Glyceraldehyde↗
Protein structure and enzyme action.
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Enzymes↗
Acid and base catalysis in a non-enzymic transfer reaction; a possible enzyme model.
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Acid-Base Equilibrium↗
Properties of the phosphorylated active site of phosphoglucomutase.
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Catalytic Domain↗
The role of water in enzymatic hydrolysis; general method and its application to myosin.
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Enzymes↗
Molecular geometry in enzyme action.
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Enzymes↗
The mechanism of the galactose-glucose interconversion in Lactobacillus bulgaricus.
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Carbohydrate Metabolism↗