Activity of NAD-dependent isocitrate dehydrogenase, isocitrate lyase, and malate dehydrogenase in Mucor circinelloides var. lusitanicus INMI under different modes of nitrogen supply

Microbiology ◽  
2008 ◽  
Vol 77 (4) ◽  
pp. 400-406 ◽  
Author(s):  
I. S. Mysyakina ◽  
N. S. Funtikova
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Mucor Circinelloides ◽  
Nitrogen Supply

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

Acetate metabolism in Escherichia coli

1978 ◽  
Vol 24 (2) ◽  
pp. 149-153 ◽  
Author(s):  
T. M. Lakshmi ◽  
Robert B. Helling
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Citrate Synthase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Acetate Metabolism ◽  
Wild Type ◽  
Intermediary Metabolites ◽  
Lyase Activity ◽  
Acetate Medium ◽  
The Glyoxylate Cycle

Levels of several intermediary metabolites were measured in cells grown in acetate medium in order to test the hypothesis that the glyoxylate cycle is repressed by phosphoenolpyruvate (PEP). Wild-type cells had less PEP than either isocitrate dehydrogenase – deficient cells (which had greater isocitrate lyase activity than the wild type) or isocitrate dehydrogenase – deficient, citrate synthase – deficient cells (which are poorly inducible). Thus induction of the glyoxylate cycle is more complicated than a simple function of PEP concentration. No correlation between enzyme activity and the level of oxaloacetate, pyruvate, or citrate was found either. Citrate was synthesized in citrate synthase – deficient mutants, possibly via citrate lyase.

Confirmation of the Synteny of the Human Genes for Cytoplasmic Isocitrate Dehydrogenase and Cytoplasmic Malate Dehydrogenase and Assignment to Chromosome 2

1974 ◽  
Vol 13 (1-2) ◽  
pp. 79-82
Author(s):  
R.P. Creagan ◽  
B. Carritt ◽  
S. Chen ◽  
R. Kucherlapati ◽  
F.A. McMorris ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Chromosome 2 ◽  
Human Genes

Effect of Proline, Betaine and Some Other Solutes on the Heat Stability of Mitochondrial Enzymes

1982 ◽  
Vol 9 (1) ◽  
pp. 47 ◽  
Author(s):  
D Nash ◽  
LG Paleg ◽  
JJ Wiskich
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Plant Mitochondria ◽  
Heat Stability ◽  
Heat Inactivation ◽  
Mitochondrial Enzymes

When isolated plant mitochondria are heated, isocitrate dehydrogenase, malate dehydrogenase and fumarase lose activity at different rates. The rate of loss of activity of each enzyme is reduced if the mitochondria are heated in the presence of proline, betaine or some other solutes; protection by proline or betaine against heat inactivation is also evident with these enzymes when they are solubilized. NAD-isocitrate dehydrogenase in pea mitochondria and NADP-dependent isocitrate dehydrogenase of pea chloroplasts are also protected by proline and betaine against inactivation when the isolated organelles are heated.

scholarly journals The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria

1968 ◽  
Vol 107 (4) ◽  
pp. 455-465 ◽  
Author(s):  
C. Chapman ◽  
W Bartley
Keyword(s):  
Cytochrome C ◽  
Glutamate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Nadh Oxidase ◽  
Isocitrate Lyase ◽  
Lag Phase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oxoglutarate Dehydrogenase ◽  
Nadh Cytochrome ◽  
Glucose 6 Phosphate Dehydrogenase

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase and NADH–cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP+-linked) and NADPH–cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD+- and NADP+-linked), α-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, α-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD+- and NADP+-linked), glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.

scholarly journals Role of Phosphoenolpyruvate in the NADP-Isocitrate Dehydrogenase and Isocitrate Lyase Reaction in Escherichia coli

2006 ◽  
Vol 189 (3) ◽  
pp. 1176-1178 ◽  
Author(s):  
Tadashi Ogawa ◽  
Keiko Murakami ◽  
Hirotada Mori ◽  
Nobuyoshi Ishii ◽  
Masaru Tomita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Isocitrate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Glyoxylate Shunt ◽  
Acid Cycle ◽  
Uncompetitive Inhibition

ABSTRACT Phosphoenolpyruvate inhibited Escherichia coli NADP-isocitrate dehydrogenase allosterically (Ki of 0.31 mM) and isocitrate lyase uncompetitively (Ki ′ of 0.893 mM). Phosphoenolpyruvate enhances the uncompetitive inhibition of isocitrate lyase by increasing isocitrate, which protects isocitrate dehydrogenase from the inhibition, and contributes to the control through the tricarboxylic acid cycle and glyoxylate shunt.

Effects of Various Solutes on the Thermostability of Isocitrate Dehydrogenase and Malate Dehydrogenase of Isolated Plant Mitochondria.

1982 ◽  
Vol 9 (6) ◽  
pp. 715 ◽  
Author(s):  
D Nash ◽  
JT Wiskich
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Choline Chloride ◽  
Plant Mitochondria ◽  
Membrane Integrity ◽  
Triticum Aestivum L ◽  
Osmotic Effect ◽  
Pisum Sativum L ◽  
Wheat Leaves ◽  
Brassica Oleracea L

Proline and betaine increased the thermostability of NAD-isocitrate dehydrogenase (EC 1.1.1.41) and of NAD-malate dehydrogenase (EC 1.1.1.37) when mitochondria isolated from pea leaves (Pisum sativum L.), wheat leaves (Triticum aestivum L.) and cauliflower buds (Brassica oleracea L.) were heated. Potassium chloride and choline chloride also increased the thermostability of isocitrate dehydrogenase in the three species, but their effects on malate dehydrogenase varied. Protection was found with both intact and disrupted mitochondria, indicating that it was not dependent on an osmotic effect. Proline and KCl also prolonged membrane integrity, as measured by impermeability to NAD+, during heating of pea leaf and cauliflower bud mitochondria. Phenylalanine reduced the thermostability of isocitrate dehydrogenase, indicating that protection is not a general solute effect.

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