Isolation and Characterization of Isocitrate Lyase and Malate Synthase from Bacillus stearothermophilus

1975 ◽  
Vol 3 (2) ◽  
pp. 303-306 ◽  
Author(s):  
R. M. CHELL ◽  
T. K. SUNDARAM
Keyword(s):  
Bacillus Stearothermophilus ◽  
Isocitrate Lyase ◽  
Malate Synthase ◽  
Isolation And Characterization

Isolation and characterization of dominant mutations resistant to carbon catabolite repression of galactokinase synthesis in Saccharomyces cerevisiae

1981 ◽  
Vol 1 (2) ◽  
pp. 83-93
Author(s):  
K Matsumoto ◽  
A Toh-e ◽  
Y Oshima
Keyword(s):  
Partial Resistance ◽  
Carbon Catabolite Repression ◽  
Glucose Repression ◽  
Isocitrate Lyase ◽  
Isolation And Characterization ◽  
Enhanced Resistance ◽  
Leloir Pathway ◽  
Resistant Mutants ◽  
A Site

Seven dominant mutations showing greatly enhanced resistance to the glucose repression of galactokinase synthesis have been isolated from GAL81 mutants, which have the constitutive phenotype but are still strongly repressible by glucose for the synthesis of the Leloir enzymes. These glucose-resistant mutants were due to semidominant mutations at either of two loci, GAL82 and GAL83. Both loci are unlinked to the GAL81- gal4, gal80, or gal7 X gal10 X gal1 locus or to each other. The GAL83 locus was mapped on chromosome V at a site between arg9 and cho1. The GAL82 and GAL83 mutations produced partial resistance of galactokinase to glucose repression only when one or both of these mutations were combined with a GAL81 or a gal80 mutation. The GAL82 and GAL83 mutations are probably specific for expression of the Leloir pathway and related enzymes, because they do not affect the synthesis of alpha-D-glucosidase, invertase, or isocitrate lyase.

Isolation and characterization of a bacteriocin produced by Bacillus stearothermophilus strain NU-10

1976 ◽  
Vol 22 (12) ◽  
pp. 1743-1750 ◽  
Author(s):  
Ronald Yule ◽  
B. D. Barridge
Keyword(s):  
Molecular Weight ◽  
Stationary Phase ◽  
Bacillus Stearothermophilus ◽  
Proteolytic Enzymes ◽  
Small Molecular Weight ◽  
Optimal Production ◽  
Chemical Treatments ◽  
Neutral Ph ◽  
Isolation And Characterization

Broth-grown cultures of Bacillus stearothermophilus strain NU-10 produce a bacteriocin which exerts lethal activity on other strains of the bacterium. Optimal production occurs during late maximum stationary phase of growth, at neutral pH, and 55–65 °C. The bacteriocin can be substantially purified by a combination of precipitations, centrifugations, and gel filtrations. The thermocin is composed of protein and carbohydrate. It is partially destroyed by proteolytic enzymes but is resistant to DNase, RNase, and various chemical treatments. The bacteriocin has a small molecular weight and exhibits considerable thermostability.

Characterization of a Bifunctional Glyoxylate Cycle Enzyme, Malate Synthase/Isocitrate Lyase, of Euglena gracilis

2011 ◽  
Vol 58 (2) ◽  
pp. 128-133 ◽  
Author(s):  
MASAMI NAKAZAWA ◽  
MASAAKI NISHIMURA ◽  
KENGO INOUE ◽  
MITSUHIRO UEDA ◽  
HIROSHI INUI ◽  
...  
Keyword(s):  
Euglena Gracilis ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Cycle Enzyme

scholarly journals Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp

1978 ◽  
Vol 173 (1) ◽  
pp. 165-177 ◽  
Author(s):  
R M Chell ◽  
T K Sundaram ◽  
A E Wilkinson
Keyword(s):  
Thermal Denaturation ◽  
Isocitrate Lyase ◽  
Homogeneous State ◽  
Thiol Groups ◽  
Thermophilic Bacillus ◽  
Relative Paucity ◽  
Salt Activation ◽  
Isolation And Characterization ◽  
Mesophilic Bacterium

Isocitrate lyase was isolated in homogeneous state from a thermophilic Bacillus. The enzyme has a mol.wt. of 180000 and a pI of 4.5 and contains threonine as the N-terminal residue. It resembles in size the cognate enzyme from the mesophilic bacterium Pseudomonas indigofera, but is smaller than the enzyme from the eukaryotic fungus Neurospora crassa. All three lyases are tetramers and similar in amino acid composition, but the thermophile enzyme is distinctive from its mesophilic coutnerparts in possessing a lower catalytic-centre activity, greater resistance to chemical and thermal denaturation and fewer thiol groups and in being strongly activated by salts. Salt activation, by 0.4M-KCl, is about 3-fold at 30 degrees C and pH 6.8 and weakens progressively as the temperature or pH is raised. The activation is probably due to a change in the enzyme conformation caused by the electrolyte modifying the interaction between charged groups or between hydrophobic groups in protein. The possible significance of the salt activation, of the relative paucity of thiol groups and of the greater resistance to chemical denaturants is discussed. Besides its effect on the Vmax., KCl produces large increases in the magnitude of several kinetic parameters. A rise in reaction temperature from 30 to 55 degrees C produces a somewhat similar result. In view of these peculiar features, the patterns of inhibition of enzyme activity by compounds such as succinate and phosphoenolpyruvate were examined at 30 and 55 degrees C in the presence and absence of KCl.

scholarly journals Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations.

1990 ◽  
Vol 172 (12) ◽  
pp. 7306-7309 ◽  
Author(s):  
J Schnier ◽  
H S Gewitz ◽  
S E Behrens ◽  
A Lee ◽  
C Ginther ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Bacillus Stearothermophilus ◽  
Isolation And Characterization ◽  
Protein Mutations
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