Molecular Mechanisms of Enzyme Activation by Monovalent Cations.
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Metals in Biology 2016: Molecular Basis of Selection of Metals by Enzymes.The contribution of two isozymes to the pyruvate kinase activity of Vibrio cholerae: One K+-dependent constitutively active and another K+-independent with essential allosteric activation.Arabidopsis β-Amylase2 Is a K+-Requiring, Catalytic Tetramer with Sigmoidal Kinetics.Sodium ions activated phosphofructokinase leading to enhanced D-lactic acid production by Sporolactobacillus inulinus using sodium hydroxide as a neutralizing agent.Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosaCation trafficking propels RNA hydrolysis
P2860
Molecular Mechanisms of Enzyme Activation by Monovalent Cations.
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Molecular Mechanisms of Enzyme Activation by Monovalent Cations.
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type
label
Molecular Mechanisms of Enzyme Activation by Monovalent Cations.
@en
prefLabel
Molecular Mechanisms of Enzyme Activation by Monovalent Cations.
@en
P2860
P356
P1476
Molecular Mechanisms of Enzyme Activation by Monovalent Cations
@en
P2093
Enrico Di Cera
P2860
P304
20840-20848
P356
10.1074/JBC.R116.737833
P407
P577
2016-07-26T00:00:00Z