“Hydroxylamine Kinase” and Pyruvic Kinase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. THE ROLE OF ADENOSINE TRIPHOSPHATE IN THE ENZYMATIC ACTIVATION OF CARBON DIOXIDE1
2. ENZYMATIC ACTIVATION OF CARBON DIOXIDE
3. Bicarbonate- and Hydroxylamine-dependent Degradation of Adenosine Triphosphate
4. Bicarbonate-dependent enzymic phosphorylation of fluoride by adenosine triphosphate
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2. Ligand-Induced Domain Movement in Pyruvate Kinase: Structure of the Enzyme from Rabbit Muscle with Mg2+, K+, andl-Phospholactate at 2.7 Å Resolution;Archives of Biochemistry and Biophysics;1997-09
3. Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate;Biochemistry;1994-05-01
4. Mammalian and avian liver phosphoenolpyruvate carboxykinase. Alternate substrates and inhibition by analogues of oxaloacetate.;Journal of Biological Chemistry;1990-05
5. N-Hydroxycarbamate is the substrate for the pyruvate kinase catalyzed phosphorylation of hydroxylamine;Biochemistry;1984-09-11
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