The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

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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.

P2860

Q40959108-245C57CB-29C3-4E47-963D-0C57C57985CE

P2860

The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

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http://www.wikidata.org/entity/Q41790315

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2014 nî lūn-bûn

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2014年の論文

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2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

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2014年论文

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The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

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label

The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

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prefLabel

The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

@en

P1476

The importance of polarity in the evolution of the K+ binding site of pyruvate kinase

@en

P2093

Carlos Guerrero-Mendiola

http://www.w3.org/2001/XMLSchema#string

Leticia Ramírez-Silva

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P2860

Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate

Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution

Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel

Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis

Sticky ions in biological systems

Water-induced transitions in the K+ requirements for the activity of pyruvate kinase entrapped in reverse micelles.

Modification of ligand binding to the Na+/K+-activated ATPase.

Selectivity of pyruvate kinase for Na+ and K+ in water/dimethylsulfoxide mixtures.

Pyruvate kinase revisited: the activating effect of K+.

Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase.

P304

22214-22226

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scholarly article

P356

10.3390/IJMS151222214

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P407

English

P433

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P478

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P50

Nallely Cabrera

P577

2014-12-02T00:00:00Z

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P5875

269181448

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P698

25474090

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P932

4284704

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The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

about

P2860

P2860

The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932