scholarly journals Regulation of ‘malic’ enzyme of Solanum tuberosum by metabolites

1974 ◽  
Vol 137 (1) ◽  
pp. 45-53 ◽  
Author(s):  
D. D. Davies ◽  
K. D. Patil
Keyword(s):  
Solanum Tuberosum ◽  
Malic Enzyme ◽  
Energy Charge ◽  
Dicarboxylic Acids ◽  
Oxidative Decarboxylation ◽  
Bivalent Cation ◽  
Ph Values ◽  
Rate Versus ◽  
Reductive Carboxylation

A purification of ‘malic’ enzyme from potato is described. The purified enzyme is specific for NADP and requires a bivalent cation for activity. At pH values below 7 the plot of rate versus malate concentration approximates to normal Michaelis–Menten kinetics. At pH values above 7 the plot of rate versus malate concentration is sigmoid. A number of dicarboxylic acids activate the enzyme and remove the sigmoidicity. The enzyme is inhibited by phosphate, triose phosphates and AMP. In general, effectors of the oxidative decarboxylation of malate behave in the same manner in the reductive carboxylation of pyruvate. The response of the enzyme to energy charge is reported and the physiological significance of the response to metabolites is discussed in relation to the proposed role of the enzyme in the control of pH.

scholarly journals Unidirectional inhibition and activation of ‘malic’ enzyme of Solanum tuberosum by meso-tartrate

1975 ◽  
Vol 149 (2) ◽  
pp. 349-355 ◽  
Author(s):  
K H Do Nascimento ◽  
D D Davies ◽  
K D Patil
Keyword(s):  
Solanum Tuberosum ◽  
Organic Acids ◽  
Malic Acid ◽  
Active Site ◽  
Malic Enzyme ◽  
Control Site ◽  
Oxidative Decarboxylation ◽  
Reductive Carboxylation ◽  
Similar Explanation ◽  
Stimulation Of

A kinetic study of ‘malic’ enzyme (EC 1.1.1.40) from potato suggests that the mechanism is Ordered Bi Ter with NADP+ binding before malate, and NADPH binding before pyruvate and HCO3-. The analysis is complicated by the non-linearity that occurs in some of the plots. meso-Tartrate is shown to inhibit the oxidative decarboxylation of malate but to activate the reductive carboxylation of pyruvate. To explain these unidirectional effects it is suggested that the control site of ‘malic’ enzyme binds organic acids (including meso-tartrate) which activate the enzyme. meso-Tartrate, however, competes with malate for the active site and thus inhibits the oxidative decarboxylation of malate. Because meso-tartrate does not compete effectively with pyruvate for enzyme-NADPH, its binding at the control site leads to a stimulation of the carboxylation of pyruvate. A similar explanation is advanced for the observation that malic acid stimulates its own synthesis.

scholarly journals Characterization of an archaeal malic enzyme from the hyperthermophilic archaeonThermococcus kodakaraensisKOD1

Archaea ◽  
2005 ◽  
Vol 1 (5) ◽  
pp. 293-301 ◽  
Author(s):  
Wakao Fukuda ◽  
Yulia Sari Ismail ◽  
Toshiaki Fukui ◽  
Haruyuki Atomi ◽  
Tadayuki Imanaka
Keyword(s):  
Enzyme Activity ◽  
Malic Enzyme ◽  
Hyperthermophilic Archaea ◽  
Oxidative Decarboxylation ◽  
Limited Information ◽  
Gene Encoding ◽  
Malic Enzyme Activity ◽  
Reductive Carboxylation ◽  
Reaction Direction

Although the interconversion between C4 and C3 compounds has an important role in overall metabolism, limited information is available on the properties and regulation of enzymes acting on these metabolites in hyperthermophilic archaea. Malic enzyme is one of the enzymes involved in this interconversion, catalyzing the oxidative decarboxylation of malate to pyruvate as well as the reductive carboxylation coupled with NAD(P)H. This study focused on the enzymatic properties and expression profile of an uncharacterized homolog of malic enzyme identified in the genome of a heterotrophic, hyperthermophilic archaeonT hermococcus kodakaraensisKOD1 (Tk-Mae). The amino acid sequence ofTk-Mae was 52–58% identical to those of malic enzymes from bacteria, whereas the similarities to the eukaryotic homologs were lower. Several catalytically important regions and residues were conserved in the primary structure ofTk-Mae. The recombinant protein, which formed a homodimer, exhibited thermostable malic enzyme activity with strict divalent cation dependency. The enzyme preferred NADP+rather than NAD+, but did not catalyze the decarboxylation of oxaloacetate, unlike the usual NADP-dependent malic enzymes. The apparent Michaelis constant (Km) ofTk-Mae for malate (16.9 mM) was much larger than those of known enzymes, leading to no strong preference for the reaction direction. Transcription of the gene encodingTk-Mae and intracellular malic enzyme activity inT. kodakaraensiswere constitutively weak, regardless of the growth substrates. Possible roles ofTk-Mae are discussed based on these results and the metabolic pathways ofT. kodakaraensisdeduced from the genome sequence.

scholarly journals Isolation and properties of a ‘malic’ enzyme from cauliflower bud mitochondria

1971 ◽  
Vol 122 (4) ◽  
pp. 495-501 ◽  
Author(s):  
A. R. Macrae
Keyword(s):  
Malic Enzyme ◽  
Tricarboxylic Acid Cycle ◽  
Decarboxylase Activity ◽  
Enzyme Preparations ◽  
Ph Values ◽  
Low Concentrations ◽  
Absolute Requirement ◽  
Nad Oxidoreductase ◽  
Regulatory Properties

1. A ‘malic’ enzyme [l-malate–NAD oxidoreductase (decarboxylating), EC 1.1.1.39] has been isolated from cauliflower bud mitochondria and partially purified. 2. The enzyme is specific for l-malate and has an absolute requirement for either Mn2+, Co2+ or Mg2+. 3. The enzyme shows activity with both NAD+ and NADP+, but NAD+ is the preferred cofactor. 4. No appreciable oxaloacetate decarboxylase activity is present in the enzyme preparations even at low pH values. 5. The enzyme is inhibited by NADH and by oxaloacetate and stimulated by SO42− and by low concentrations of CoA. 6. The regulatory properties of the enzyme support the proposed role of the enzyme in the utilization of tricarboxylic acid-cycle acids for energy production when glycolysis is suppressed.

Possible regulatory roles of ATP:citrate lyase, malic enzyme, and AMP deaminase in lipid accumulation by Rhodosporidium toruloides CBS 14

1985 ◽  
Vol 31 (11) ◽  
pp. 1000-1005 ◽  
Author(s):  
Christopher Thomas Evans ◽  
Colin Ratledge
Keyword(s):  
Lipid Accumulation ◽  
Malic Enzyme ◽  
Energy Charge ◽  
Molecular Size ◽  
Rhodosporidium Toruloides ◽  
Regulatory Control ◽  
Central Position ◽  
Amp Deaminase ◽  
Atp:Citrate Lyase

The properties of ATP:citrate lyase, malic enzyme, and AMP deaminase have been investigated in Rhodosporidium toruloides CBS 14. ATP:citrate lyase had a molecular size of 480 000 daltons and apparent Km for citrate and ATP of 0.19 mM and 0.15 mM, respectively. The enzyme was inhibited by ADP, glucose 6-phosphate, palmitoyl-CoA, and oleoyl-CoA. [Formula: see text] ions showed a 95% stimulation of activity at nonsaturating concentrations (0.1 mM) of citrate. Malic enzyme had a molecular size of 205 000 daltons and an apparent Km for malate of 0.7 mM. The enzyme was only weakly inhibited by citrate, pyruvate, oxaloacetate, and ATP but no metabolite was found which exerted a significant regulatory control over the enzyme. However this enzyme could be used as the principal, if not sole, source of NADPH needed for fatty acid biosynthesis. The role of this enzyme and the central position of malate as a key metabolite in determining how lipid accumulation could be initiated and then sustained is discussed. AMP deaminase was detected in low activities but was fourfold higher in nitrogen-limited cells. The possible role of this enzyme in degrading AMP, regulating cellular energy charge, and supplementing [Formula: see text] pools in this yeast is also discussed.

scholarly journals The role of malic enzyme in the regulation of lipid accumulation in filamentous fungi

Microbiology ◽  
1999 ◽  
Vol 145 (8) ◽  
pp. 1911-1917 ◽  
Author(s):  
James P. Wynn ◽  
Aidil bin Abdul Hamid ◽  
Colin Ratledge
Keyword(s):  
Filamentous Fungi ◽  
Lipid Accumulation ◽  
Malic Enzyme

scholarly journals The role of pH on the survival of rumen protozoa in steers

2010 ◽  
Vol 39 (10) ◽  
pp. 2262-2267 ◽  
Author(s):  
Raul Franzolin ◽  
Burk A. Dehority
Keyword(s):  
Experimental Period ◽  
Adaptation Period ◽  
Individual Animal ◽  
Effect Of Ph ◽  
Ph Values ◽  
Rumen Protozoa ◽  
Rumen Ph ◽  
Sampling Times ◽  
Ciliate Protozoa

In order to study the effect of pH on defaunation in the rumen, four rumen fistulated steers were fed a basal roughage diet for a 4-week adaptation period followed by 17 weeks of feeding with three diets and two feeding levels of high concentrate diet. Rumen outflow fluid rate was evaluated in both ration levels. Rumen protozoa population was monitored weekly and when animals became defaunated, protozoa were reinoculated with rumen contents from one of the faunated steers. At every two weeks, during all the experimental period, rumen pH was measured in all animals at 0, 4, 8 and 12 h after feeding. It was observed an individual animal influence on the establishment and maintenance of the rumen ciliate protozoa population. In all sampling times, mean rumen pH values were higher in faunated steers than in the defaunated ones. No differences were observed in rumen outflow fluid rates between the two ration levels. Extended periods of low rumen pH are probably more detrimental to the survival of ciliate protozoa in the rumen than other factors.

scholarly journals Glucose stimulates transcription of fatty acid synthase and malic enzyme in avian hepatocytes

1998 ◽  
Vol 274 (3) ◽  
pp. E493-E501 ◽  
Author(s):  
F. Bradley Hillgartner ◽  
Tina Charron
Keyword(s):  
Fatty Acid ◽  
High Fat Diet ◽  
Malic Enzyme ◽  
Fatty Acid Synthase ◽  
Primary Cultures ◽  
Pentose Phosphate ◽  
Mrna Abundance ◽  
Low Fat Diet ◽  
Low Carbohydrate

Transcription of fatty acid synthase (FAS) and malic enzyme (ME) in avian liver is low during starvation or feeding a low-carbohydrate, high-fat diet and high during feeding a high-carbohydrate, low-fat diet. The role of glucose in the nutritional control of FAS and ME was investigated by determining the effects of this metabolic fuel on expression of FAS and ME in primary cultures of chick embryo hepatocytes. In the presence of triiodothyronine, glucose (25 mM) stimulated an increase in the activity and mRNA abundance of FAS and ME. These effects required the phosphorylation of glucose to glucose 6-phosphate but not further metabolism downstream of the aldolase step of the glycolytic pathway. Xylitol mimicked the effects of glucose on FAS and ME expression, suggesting that an intermediate of the pentose phosphate pathway may be involved in mediating this response. The effects of glucose on the mRNA abundance of FAS and ME were accompanied by similar changes in transcription of FAS and ME. These data support the hypothesis that glucose plays a role in mediating the effects of nutritional manipulation on transcription of FAS and ME in liver.

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