(Q27635230)

2

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A M Lambeir

3

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D M Antonov

4

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K Augustyns

5

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R K Wierenga

Enzyme catalysis: not different, just better

6

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language of work or name

English

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publication date

October 2001

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published in

FEBS Journal

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volume

268

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page(s)

5189-96

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issue

19

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cites work

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Computer simulation of the triosephosphate isomerase catalyzed reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Triosephosphate isomerase requires a positively charged active site: the role of lysine-12

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

The role of water in the catalytic efficiency of triosephosphate isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Proton transfer in the mechanism of triosephosphate isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

AMoRe: an automated package for molecular replacement

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Automated protein model building combined with iterative structure refinement

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Improved methods for building protein models in electron density maps and the location of errors in these models

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

PROCHECK: a program to check the stereochemical quality of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

WHAT IF: a molecular modeling and drug design program

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Low-barrier hydrogen bonds and enzymic catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

The low barrier hydrogen bond in enzymatic catalysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

The enhancement of enzymatic rate accelerations by Brønsted acid-base catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Structure of yeast triosephosphate isomerase at 1.9-A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 m-ammonium sulphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.0014-2956.2001.02452.X

10.1046/J.0014-2956.2001.02452.X

21 January 2018

Identifiers

DOI

0 references

Fatcat ID

release_r4qvn7gnrveg7izwy4lgnxsnoa

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/r4qvn7gnrveg7izwy4lgnxsnoa