Isocitrate lyase in Coprinus lagopus (sensu Buller)

1969 ◽  
Vol 15 (6) ◽  
pp. 637-640 ◽  
Author(s):  
P. J. Casselton ◽  
M. O. Fawole ◽  
L. A. Casselton
Keyword(s):  
Carbon Source ◽  
Isocitrate Lyase ◽  
Glucose Medium ◽  
Lyase Activity ◽  
Acetate Medium

Isocitrate lyase activity was detected in cell-free extracts of both a monokaryon and a dikaryon of Coprinus lagopus sensu Buller grown in media containing either acetate or glucose as carbon source. The activity in extracts of mycelium grown in an acetate medium was greater than that in extracts of mycelium grown in a glucose medium but marked differences between extracts of monokaryons and dikaryons grown in similar media were not observed. The isocitrate lyase activity could be largely sedimented by centrifugation at 10 000 × g for 20 minutes.

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.

scholarly journals Isocitrate Lyase Activity in Lactobacillus murinus CNRZ 313

1983 ◽  
Vol 66 (6) ◽  
pp. 1232-1236 ◽  
Author(s):  
M.C. Albizzatti de Rivadeneira ◽  
M.C. Manca de Nadra ◽  
A.A. Pesce de Ruiz Holgado ◽  
G. Oliver
Keyword(s):  
Isocitrate Lyase ◽  
Lyase Activity ◽  
Lactobacillus Murinus

Lag, adaptation and ageing in a micro-organism ( Bact. lactis aerogenes )

1961 ◽  
Vol 155 (959) ◽  
pp. 195-201 ◽  
Keyword(s):  
Carbon Source ◽  
Generation Time ◽  
Sole Carbon Source ◽  
The Other ◽  
Lag Phase ◽  
Glucose Medium ◽  
Galactosidase Activity ◽  
Aerobacter Aerogenes ◽  
Isomerase Activity

The lag preceding growth of Bact. lactis aerogenes (Aerobacter aerogenes) after a first transfer to a medium containing D-arabinose as sole carbon source increases with the age and decreases with the size of the inoculum. During the long lag phase the β -galactosidase activity declines steeply. In contrast with this (and with a control ageing in a glucose medium) the D-ribulose isomerase activity is maintained, although no detectable consumption of D-arabinose occurs. If the long lag of unadapted cells in D-arabinose is divided into parts by intermediate passages in glucose or lactose media, the sum of the partial lags is nearly constant and equal to that observed when there is no interruption. But the periodic passages in the other media increase the rate at which growth eventually occurs in the D-arabinose. It is concluded that during the lag a decay of the enzymes in general occurs concomitantly with the development of the specific mechanisms concerned in the utilization of the new substrate. The balance of these processes (together with varying loss or retention of diffusible metabolites) is largely responsible for the observed variations in lag and mean generation time.

Metabolism of Food Reserves in Germinating Velvetleaf

Weed Science ◽  
1970 ◽  
Vol 18 (5) ◽  
pp. 565-571
Author(s):  
J. A. Mulliken ◽  
C. A. Kust ◽  
L. E. Schrader
Keyword(s):  
Hydrogen Cyanide ◽  
Isocitrate Lyase ◽  
Dry Weight ◽  
Maximal Activity ◽  
Radicle Growth ◽  
Fat Mobilization ◽  
Lyase Activity ◽  
Radicle Emergence ◽  
Weight Protein ◽  
Food Reserves

Endosperm dry weight, protein, and fat losses accompanied rapid radicle growth of velvetleaf (Abutilon theophrasti Medic.) between 12 and 36 hr of germination at 31 C. Cotyledonary reserves were mobilized after 36 hr. Isocitrate lyase activity sedimented with a particulate fraction in varying degrees, but maximal activity developed at times coincident with fat mobilization. Respiration of excised endosperms reached maximal rates shortly after radicle emergence. The actions of hydrogen cyanide, carbon monoxide, and 2,4-dinitrolphenol indicated that respiration of endosperms excised from imbibed and germinated seed was due to cytochrome oxidase activity, and was coupled to phosphorylation.

scholarly journals The Saccharomyces cerevisiae ICL2 Gene Encodes a Mitochondrial 2-Methylisocitrate Lyase Involved in Propionyl-Coenzyme A Metabolism

2000 ◽  
Vol 182 (24) ◽  
pp. 7007-7013 ◽  
Author(s):  
Marijke A. H. Luttik ◽  
Peter Kötter ◽  
Florian A. Salomons ◽  
Ida J. van der Klei ◽  
Johannes P. van Dijken ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nitrogen Source ◽  
Coenzyme A ◽  
Isocitrate Lyase ◽  
Significant Activity ◽  
Mrna Levels ◽  
Wild Type ◽  
Cell Extracts ◽  
Lyase Activity ◽  
Null Mutants

ABSTRACT The Saccharomyces cerevisiae ICL1 gene encodes isocitrate lyase, an essential enzyme for growth on ethanol and acetate. Previous studies have demonstrated that the highly homologousICL2 gene (YPR006c) is transcribed during the growth of wild-type cells on ethanol. However, even when multiple copies are introduced, ICL2 cannot complement the growth defect oficl1 null mutants. It has therefore been suggested thatICL2 encodes a nonsense mRNA or nonfunctional protein. In the methylcitrate cycle of propionyl-coenzyme A metabolism, 2-methylisocitrate is converted to succinate and pyruvate, a reaction similar to that catalyzed by isocitrate lyase. To investigate whetherICL2 encodes a specific 2-methylisocitrate lyase, isocitrate lyase and 2-methylisocitrate lyase activities were assayed in cell extracts of wild-type S. cerevisiae and of isogenicicl1, icl2, and icl1 icl2 null mutants. Isocitrate lyase activity was absent in icl1 andicl1 icl2 null mutants, whereas in contrast, 2-methylisocitrate lyase activity was detected in the wild type and single icl mutants but not in the icl1 icl2mutant. This demonstrated that ICL2 encodes a specific 2-methylisocitrate lyase and that the ICL1-encoded isocitrate lyase exhibits a low but significant activity with 2-methylisocitrate. Subcellular fractionation studies and experiments with an ICL2-green fluorescent protein fusion demonstrated that theICL2-encoded 2-methylisocitrate lyase is located in the mitochondrial matrix. Similar to that of ICL1, transcription of ICL2 is subject to glucose catabolite repression. In glucose-limited cultures, growth with threonine as a nitrogen source resulted in a ca. threefold induction ofICL2 mRNA levels and of 2-methylisocitrate lyase activity in cell extracts relative to cultures grown with ammonia as the nitrogen source. This is consistent with an involvement of the 2-methylcitrate cycle in threonine catabolism.

Apparent isocitrate lyase activity in Leishmania amazonensis

2017 ◽  
Vol 62 (4) ◽  
Author(s):  
Concepción Hernández-Chinea ◽  
Laura Maimone ◽  
Yelitza Campos ◽  
Walter Mosca ◽  
Pedro J. Romero
Keyword(s):  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Leishmania Amazonensis ◽  
Lyase Activity

AbstractEarly reports have demonstrated the occurrence of glyoxylate cycle enzymes in several

Incomplete Glyoxysomes Appearing at a Late Stage of Maturation of Cucumber Seeds

1979 ◽  
Vol 34 (12) ◽  
pp. 1232-1236 ◽  
Author(s):  
Wolfram Koller ◽  
Jürgen Frevert ◽  
Helmut Kindi
Keyword(s):  
Late Stage ◽  
Citrate Synthase ◽  
De Novo ◽  
Density Gradient Centrifugation ◽  
Isocitrate Lyase ◽  
Gradient Centrifugation ◽  
Protein Body ◽  
Electrophoretic Analysis ◽  
Malate Synthase ◽  
Lyase Activity

Seeds of cucumber fruits at a late stage of ripening were analyzed for microbodies and micro­body components. On isopycnic density gradient centrifugation of homogenates in the presence of EDTA, several particulate fractions were obtained: a light membraneous fraction (density d = 1.09-1.11 kg × 1-1), a mitochondria-enriched fraction (d = 1.21 kg × 1-1), a microbody-enriched fraction (d = 1.23 kg × 1-1), and a protein body fraction (d= 1.26 - 1.29 kg × 1-1). Microbo­dies were revealed by exactly coinciding peaks of malate synthase, catalase and crotonase; small proportions of citrate synthase and malate dehydrogenase were also present in this zone. Isocitrate lyase activity, however, did not occur in the seeds at this stage. The examination of enzyme activi­ties indicated the presence of microbodies which cannot function as competent glyoxysomes be­cause of the lack of isocitrate lyase. Moreover, de novo synthesis from [3H] leucine could be de­monstrated for malate synthase by means of immunoprecipitation of newly synthesized malate synthase and subsequent electrophoretic analysis.

scholarly journals Control of isocitrate lyase synthesis in Chlorella fusca var. vacuolata. Rate of enzyme synthesis in the presence and absence of acetate measured by [35S]methionine labelling and immunoprecipitation

1978 ◽  
Vol 176 (1) ◽  
pp. 179-185 ◽  
Author(s):  
S M Dunham ◽  
C F Thurston
Keyword(s):  
Isocitrate Lyase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Synthesis ◽  
Acetate Incorporation ◽  
Enzyme Protein ◽  
Chlorella Fusca ◽  
Rate Of Increase ◽  
Lyase Activity ◽  
Presence And Absence

The rate of increase of isocitrate lyase activity was measured in darkened Chlorella fusca var. vaculoata cultures in the presence and absence of acetate and compared with the rate of incorporation of [35S]methionine into isocitrate lyase enzyme protein under the same conditions. Isocitrate lyase enzyme protein was isolated for this purpose by specific immunoprecipitation and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. After 4h in the dark, in the presence of acetate the rate of increase of isocitrate lyase activity was 75 times that in the absence of acetate. Incorporation of [35S]methionine into isocitrate lyase was 140 times greater in the presence of acetate. Incorporation of [35S]methionine into the trichloroacetic acid-insoluble fraction overall was about five times as fast in the presence of acetate. These data are not consistent with an increased turnover of isocitrate lyase enzyme molecules, sufficient to account for the low rate of increase of isocitrate lyase activity in the absence of acetate. The greater rate of enzyme synthesis in the presence of acetate must therefore be due to some effect of this metabolite on the processing or translation of isocitrate lyase mRNA.

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