A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate - Wikidata - wikimedia - TriplyDB

A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate

A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate

http://www.wikidata.org/entity/Q35221157

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On the Kinetic and Allosteric Regulatory Properties of the ADP-Glucose Pyrophosphorylase from Rhodococcus jostii: An Approach to Evaluate Glycogen Metabolism in Oleaginous Bacteria.Allosteric Control of Substrate Specificity of the Escherichia coli ADP-Glucose Pyrophosphorylase.

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P2860

A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate

http://www.wikidata.org/entity/Q35221157

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

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

@wuu

name

A novel dual allosteric activa ...... horylase: the role of pyruvate

@ast

A novel dual allosteric activa ...... horylase: the role of pyruvate

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type

label

A novel dual allosteric activa ...... horylase: the role of pyruvate

@ast

A novel dual allosteric activa ...... horylase: the role of pyruvate

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prefLabel

A novel dual allosteric activa ...... horylase: the role of pyruvate

@ast

A novel dual allosteric activa ...... horylase: the role of pyruvate

@en

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JOURNAL.PONE.0103888

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A novel dual allosteric activa ...... horylase: the role of pyruvate

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Mabel C Aleanzi

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Matías D Asención Diez

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P2860

ExPASy: The proteomics server for in-depth protein knowledge and analysis

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Structural analysis of ADP-glucose pyrophosphorylase from the bacterium Agrobacterium tumefaciens

Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylase

Crystal structure of potato tuber ADP-glucose pyrophosphorylase.

The ancestral activation promiscuity of ADP-glucose pyrophosphorylases from oxygenic photosynthetic organisms.

ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis.

Insights into glycogen metabolism in chemolithoautotrophic bacteria from distinctive kinetic and regulatory properties of ADP-glucose pyrophosphorylase from Nitrosomonas europaea.

Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli.

Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme.

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e103888

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scholarly article

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10.1371/JOURNAL.PONE.0103888

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8

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9

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Miguel A Ballicora

Alberto A Iglesias

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2014-08-07T00:00:00Z

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264637565

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25102309

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4125136

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