PDC1/YLR044C Literature Guide Help

Other names published for PDC1: indolepyruvate decarboxylase 1, YLR044C

PDC1 - Protein/Nucleic Acid Structure (12)

ReferenceOther Genes Addressed
Shrestha A, et al.  (2010) Modeling of pyruvate decarboxylases from ethanol producing bacteria. Bioinformation 4(8):378-84
Kutter S, et al.  (2009) Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation. J Biol Chem 284(18):12136-44
Stevenson BJ, et al.  (2008) Directed evolution of yeast pyruvate decarboxylase 1 for attenuated regulation and increased stability. Biochemistry 47(9):3013-25
Kutter S, et al.  (2006) The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis. FEBS J 273(18):4199-209
Casas JS, et al.  (2004) The reaction of dimethyltin(IV) dichloride with thiamine diphosphate (H2TDP): synthesis and structure of [SnMe2(HTDP)(H2O)]Cl.H2O, and possibility of a hitherto unsuspected role of the metal cofactor in the mechanism of vitamin-B1-dependent enzymes. Inorg Chem 43(6):1957-63
Nemeria N, et al.  (2004) Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme. Biochemistry 43(21):6565-75
Jordan F, et al.  (2002) Spectroscopic evidence for participation of the 1',4'-imino tautomer of thiamin diphosphate in catalysis by yeast pyruvate decarboxylase. Bioorg Chem 30(3):188-98
Sergienko EA and Jordan F  (2002) New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme. Biochemistry 41(12):3952-67
Liu M, et al.  (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions. Biochemistry 40(25):7355-68
Sergienko EA and Jordan F  (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values. Biochemistry 40(25):7382-403
Konig S, et al.  (1992) Synchrotron radiation solution X-ray scattering study of the pH dependence of the quaternary structure of yeast pyruvate decarboxylase. Biochemistry 31(37):8726-31
Dyda F, et al.  (1990) Preliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers' yeast. J Biol Chem 265(29):17413-5