(Q27618131)

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

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

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4

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author name string

J C Williams

1

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J P Zeelen

2

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G Neubauer

3

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J Backmann

5

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P A Michels

6

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A M Lambeir

7

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R K Wierenga

8

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publication date

March 1999

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Protein Engineering Design and Selection

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12

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243-50

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3

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Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

1 reference

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Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

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Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase

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Formation and stability of beta-hairpin structures in polypeptides

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The CCP4 suite: programs for protein crystallography

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Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57.

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Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interacti

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Protein sequencing by tandem mass spectrometry

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

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Experimentally observed conformation-dependent geometry and hidden strain in proteins

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Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.

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Enzyme catalysis: not different, just better

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

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Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

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

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Stabilization of protein structures

1 reference

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Structure of yeast triosephosphate isomerase at 1.9-A resolution

1 reference

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Stabilization of human triosephosphate isomerase by improvement of the stability of individual alpha-helices in dimeric as well as monomeric forms of the protein

1 reference

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Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme

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Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

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A general and fast method to generate multiple site directed mutations

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AMoRe: an automated package for molecular replacement

1 reference

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

1 reference

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Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution

1 reference

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

1 reference

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21 January 2018

Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies

1 reference

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A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.

1 reference

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21 January 2018

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Conjugate-direction minimization: an improved method for the refinement of macromolecules

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Engineering an enzyme to resist boiling

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

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Favourable native-like helical local interactions can accelerate protein folding

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Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory.

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WHAT IF: a molecular modeling and drug design program

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Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

1 reference

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The structure and function of proline-rich regions in proteins

1 reference

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Analytical properties of the nanoelectrospray ion source

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Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima

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In vitro evolution of thermodynamically stable turns

1 reference

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In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core

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

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21 January 2018

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