Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.

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Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Crystal structures of two mono ...... -arabinose isomerase activity.

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Crystal structures of two mono ...... -arabinose isomerase activity.

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Crystal structures of two mono ...... -arabinose isomerase activity.

@en

Crystal structures of two mono ...... -arabinose isomerase activity.

@nl

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Crystal structures of two mono ...... -arabinose isomerase activity.

@en

Crystal structures of two mono ...... -arabinose isomerase activity.

@nl

P1476

Crystal structures of two mono ...... L-arabinose isomerase activity

@en

P2093

Mirja Krause

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Rik K Wierenga

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Tiila Riikka Kiema

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P2860

Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle

MolProbity: all-atom structure validation for macromolecular crystallography

Structural determinants for ligand binding and catalysis of triosephosphate isomerase

The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis

Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state

Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution

Functional role of the conserved active site proline of triosephosphate isomerase

Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM

Structure-based protein engineering efforts with a monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties

Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex

P304

490-499

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P31

scholarly article

P356

10.1107/S2053230X16007548

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P433

Pt 6

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P478

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P50

Peter Neubauer

P577

2016-05-23T00:00:00Z

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P698

27303904

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P921

directed evolution

crystal structure

P932

4909251

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