TKL1/YPR074C Literature Guide Help

Other names published for TKL1: transketolase TKL1, YPR074C

TKL1 - Substrates/Ligands/Cofactors (32)

Results: 1 - 30 of 32 records
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ReferenceOther Genes Addressed
Solovjeva ON, et al.  (2012) Effects of free Ca(2)(+) on kinetic characteristics of holotransketolase. Protein J 31(2):137-40
Charmantray F, et al.  (2010) Fluorogenic substrates for the screening assay of transketolase through beta-elimination of umbelliferone--Development, scope and limitations. J Biotechnol 145(4):359-66
Toivari MH, et al.  (2010) Enhancing the flux of D-glucose to the pentose phosphate pathway in Saccharomyces cerevisiae for the production of D-ribose and ribitol. Appl Microbiol Biotechnol 85(3):731-9
Esakova OA, et al.  (2009) Halogenated Pyruvate Derivatives as Substrates of Transketolase from Saccharomyces cerevisiae. Biochemistry (Mosc) 74(11):1234-8
Sevostyanova I, et al.  (2009) Half-of-the-sites reactivity of transketolase from Saccharomyces cerevisiae. Biochem Biophys Res Commun 379(4):851-4
Sevostyanova IA, et al.  (2009) Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae. Biochemistry (Mosc) 74(7):789-92
Simon G, et al.  (2009) Amino acid precursors for the detection of transketolase activity in Escherichia coli auxotrophs. Bioorg Med Chem Lett 19(14):3767-70
Meshalkina LE, et al.  (2008) New evidence for cofactor's amino group function in thiamin catalysis by transketolase. Biochem Biophys Res Commun 366(3):692-7
Sevostyanova IA, et al.  (2008) Effect of bivalent cations on the interaction of transketolase with its donor substrate. Proteins 71(2):541-5
Ospanov R, et al.  (2006) Theoretical model of interactions between ligand-binding sites in a dimeric protein and its application for the analysis of thiamine diphosphate binding to yeast transketolase. Biophys Chem 124(2):106-14
Sevostyanova IA, et al.  (2006) Two methods for determination of transketolase activity. Biochemistry (Mosc) 71(5):560-2
Esakova OA, et al.  (2005) Effect of transketolase substrates on holoenzyme reconstitution and stability. Biochemistry (Mosc) 70(7):770-6
Esakova OA, et al.  (2005) Effects of transketolase cofactors on its conformation and stability. Life Sci 78(1):8-13
Golbik R, et al.  (2005) Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae. FEBS J 272(6):1326-42
Esakova OA, et al.  (2004) Donor substrate regulation of transketolase. Eur J Biochem 271(21):4189-94
Selivanov VA, et al.  (2004) Kinetic study of the H103A mutant yeast transketolase. FEBS Lett 567(2-3):270-4
Sevostyanova IA, et al.  (2004) A hitherto unknown transketolase-catalyzed reaction. Biochem Biophys Res Commun 313(3):771-4
Kovina MV, et al.  (2002) The origin of the absorption band induced through the interaction between apotransketolase and thiamin diphosphate. Biochem Biophys Res Commun 294(1):155-60
Bykova IA, et al.  (2001) One-substrate transketolase-catalyzed reaction. Biochem Biophys Res Commun 280(3):845-7
Fiedler E, et al.  (2001) Examination of donor substrate conversion in yeast transketolase. J Biol Chem 276(19):16051-8
Nilsson U, et al.  (1998) Asp477 is a determinant of the enantioselectivity in yeast transketolase. FEBS Lett 424(1-2):49-52
Meshalkina L, et al.  (1997) Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis. Eur J Biochem 244(2):646-52
Nilsson U, et al.  (1997) Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis. J Biol Chem 272(3):1864-9
Wikner C, et al.  (1995) His103 in yeast transketolase is required for substrate recognition and catalysis. Eur J Biochem 233(3):750-5
Konig S, et al.  (1994) Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate. J Biol Chem 269(14):10879-82
Wikner C, et al.  (1994) Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis. J Biol Chem 269(51):32144-50
Muller YA, et al.  (1993) A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1(2):95-103
Kuimov AN, et al.  (1986) [Functional carboxylic group in the active center of transketolase] Biokhimiia 51(11):1908-18
Usmanov RA and Kochetov GA  (1983) [Function of the arginine residue in the active center of baker's yeast transketolase] Biokhimiia 48(5):772-81
Kochetov GA, et al.  (1975) The binding of thiamine pyrophosphate with transketolase in equilibrium conditions. Biochem Biophys Res Commun 63(4):924-30
Results: 1 - 30 of 32 records
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