FBA1/YKL060C Literature Guide Help

Other names published for FBA1: LOT1, fructose-bisphosphate aldolase FBA1, YKL060C

FBA1 - Substrates/Ligands/Cofactors (18)

ReferenceOther Genes Addressed
Wang S, et al.  (2011) Switch between Life History Strategies Due to Changes in Glycolytic Enzyme Gene Dosage in Saccharomyces cerevisiae. Appl Environ Microbiol 77(2):452-9
Fendt SM, et al.  (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356
Mabiala-Bassiloua CG, et al.  (2008) Separate synthesis and evaluation of glucitol bis-phosphate and mannitol bis-phosphate, as competitive inhibitors of fructose bis-phosphate aldolases. Bioorg Med Chem Lett 18(5):1735-7
Mashego MR, et al.  (2005) Changes in the metabolome of Saccharomyces cerevisiae associated with evolution in aerobic glucose-limited chemostats. FEMS Yeast Res 5(4-5):419-30
King DA, et al.  (2004) HOCl-mediated cell death and metabolic dysfunction in the yeast Saccharomyces cerevisiae. Arch Biochem Biophys 423(1):170-81
Matic S, et al.  (2001) Interaction between phosphofructokinase and aldolase from Saccharomyces cerevisiae studied by aqueous two-phase partitioning. J Chromatogr B Biomed Sci Appl 751(2):341-8
Teusink B, et al.  (2000) Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry. Eur J Biochem 267(17):5313-29
Lobo Z  (1984) Saccharomyces cerevisiae aldolase mutants. J Bacteriol 160(1):222-6
Belasco JG and Knowles JR  (1983) Polarization of substrate carbonyl groups by yeast aldolase: investigation by Fourier transform infrared spectroscopy. Biochemistry 22(1):122-9
Kadonaga JT and Knowles JR  (1983) Role of mono- and divalent metal cations in the catalysis by yeast aldolase. Biochemistry 22(1):130-6
Smith GM and Mildvan AS  (1981) Nuclear magnetic resonance and chemical modification studies of the role of the metal in yeast aldolase. Biochemistry 20(15):4340-6
Midelfort CF, et al.  (1976) Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolases. Biochemistry 15(10):2178-85
Rabega C, et al.  (1976) [Study of purified aldolase from Saccharomyces cerevisiae, using irradiated fructose-1,6-diphosphate] Rev Ig Bacteriol Virusol Parazitol Epidemiol Pneumoftiziol Bacteriol Virusol 21(1):37-41
Schray KJ, et al.  (1975) The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions. J Biol Chem 250(13):4883-7
VANDERHEIDEN BS, et al.  (1962) The preparation and properties of crystalline yeast aldolase. J Biol Chem 237:2095-8
RICHARDS OC and RUTTER WJ  (1961) Comparative properties of yeast and muscle aldolase. J Biol Chem 236:3185-92
RICHARDS OC and RUTTER WJ  (1961) Preparation and properties of yeast aldolase. J Biol Chem 236():3177-84
ROSE IA and RIEDER SV  (1958) Studies on the mechanism on the aldolase reaction; isotope exchange reactions of muscle and yeast aldolase. J Biol Chem 231(1):315-29