Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power (Q27618131)

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

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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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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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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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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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Stabilization of protein structures

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Structure of yeast triosephosphate isomerase at 1.9-A resolution

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

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

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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

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

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

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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

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