Literature: Triosephosphate isomerase (IPR000652)
References used in this entry
The following publications were referred to in the abstract:
Enzyme catalysis: not different, just better.
Nature 350 121-4 1991
PMID: 2005961 Related citations
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA.
Biochemistry 29 6609-18 1990
PMID: 2204417 Related citations
Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Jogl G, Rozovsky S, McDermott AE, Tong L.
Proc. Natl. Acad. Sci. U.S.A. 100 50-5 2003
PMID: 12509510 Related citations
Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease.
Olah J, Orosz F, Keseru GM, Kovari Z, Kovacs J, Hollan S, Ovadi J.
Biochem. Soc. Trans. 30 30-8 2002
PMID: 12023819 Related citations
One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
Nagano N, Orengo CA, Thornton JM.
J. Mol. Biol. 321 741-65 2002
PMID: 12206759 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
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.
Alahuhta M, Salin M, Casteleijn MG, Kemmer C, El-Sayed I, Augustyns K, Neubauer P, Wierenga RK.
Protein Eng. Des. Sel. 21 257-66 2008
PMID: 18239072 Related citations
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.
Alahuhta M, Casteleijn MG, Neubauer P, Wierenga RK.
Acta Crystallogr. D Biol. Crystallogr. 64 178-88 2008
PMID: 18219118 Related citations
Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.
Gayathri P, Banerjee M, Vijayalakshmi A, Balaram H, Balaram P, Murthy MR.
Acta Crystallogr. D Biol. Crystallogr. 65 847-57 2009
PMID: 19622869 Related citations
The folding pathway of triosephosphate isomerase.
Zarate-Perez F, Chanez-Cardenas ME, Vazquez-Contreras E.
Prog Mol Biol Transl Sci 84 251-67 2008
PMID: 19121704 Related citations
Disulfide bridges in the mesophilic triosephosphate isomerase from Giardia lamblia are related to oligomerization and activity.
Reyes-Vivas H, Diaz A, Peon J, Mendoza-Hernandez G, Hernandez-Alcantara G, De la Mora-De la Mora I, Enriquez-Flores S, Dominguez-Ramirez L, Lopez-Velazquez G.
J. Mol. Biol. 365 752-63 2007
PMID: 17095008 Related citations