Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis

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The Role of Cysteine Residues in Catalysis of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis.

P2860

Q36264014-3AD91528-737A-45BF-929D-574E0B4A17BE

P2860

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis

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2015 nî lūn-bûn

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2015 թուականին հրատարակուած գիտական յօդուած

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2015 թվականին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

@en

Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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Structural and functional stud ...... rom Mycobacterium tuberculosis

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P1476

Structural and functional stud ...... rom Mycobacterium tuberculosis

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P2093

Iva Pichová

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

Jan Snášel

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

Jiří Brynda

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

Jiří Dostál

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

Ján Tarábek

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

Lucie Bednárová

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

Mahavir Singh

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P2860

Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site

Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 A resolution

The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)

Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid

Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection

The Ω-Loop Lid Domain of Phosphoenolpyruvate Carboxykinase Is Essential for Catalytic Function

Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold

XDS

Structure validation by Calpha geometry: phi,psi and Cbeta deviation

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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e0120682

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scholarly article

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10.1371/JOURNAL.PONE.0120682

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P407

English

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P478

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Ondřej Vaněk

Jindrich Fanfrlík

Iva Machová

P577

2015-03-23T00:00:00Z

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P5875

275028011

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P698

25798914

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P921

Mycobacterium tuberculosis

P932

4370629

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Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis

about

P2860

P2860

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932