scholarly journals Oxaloacetate decarboxylase activity in chickpea leaves

2020 ◽  
Vol 4 (4) ◽  
pp. 33-37
Author(s):  
S.V. Musayeva-H.G. Babayev
Keyword(s):  
Decarboxylase Activity ◽  
Oxaloacetate Decarboxylase

A Stable Miniature Protein with Oxaloacetate Decarboxylase Activity

ChemBioChem ◽  
2004 ◽  
Vol 5 (8) ◽  
pp. 1075-1080 ◽  
Author(s):  
Chris J. Weston ◽  
Charly H. Cureton ◽  
Melanie J. Calvert ◽  
Oliver S. Smart ◽  
Rudolf K. Allemann
Keyword(s):  
Decarboxylase Activity ◽  
Oxaloacetate Decarboxylase

scholarly journals Nicotinamide-adenine dinucleotide-linked “malic” enzyme in flight muscle of the tse-tse fly (Glossina) and other insects

1976 ◽  
Vol 160 (2) ◽  
pp. 253-262 ◽  
Author(s):  
J B Hoek ◽  
D J Pearson ◽  
N K Olembo
Keyword(s):  
Malate Dehydrogenase ◽  
Malic Enzyme ◽  
Flight Muscle ◽  
Intracellular Localization ◽  
Deae Cellulose ◽  
Partial Purification ◽  
Decarboxylase Activity ◽  
Matrix Space ◽  
Oxaloacetate Decarboxylase ◽  
Ph Optimum

1. A high activity of NAD-linked ‘malic’ enzyme was found in homogenates of flight muscle of different species of tse-tse fly (Glossina). The activity was the same as, or higher than, that of malate dehydrogenase and more than 20-fold that of NADP-linked ‘malic’ enzyme. A similar enzyme was found in the flight muscle of all other insects investigated, but at much lower activities. 2. ACa2+-stimulated oxaloacetate decarboxylase activity was present in all insect flight-muscle preparations investigated, in constant proportion to the NAD-linked ‘malic’ enzyme. 3. A partial purification of the NAD-linked ‘malic’ enzyme from Glossina was effected by DEAE-cellulose chromatography, which separated the enzyme from malate dehydrogenase and NADP-linked ‘malic’ enzyme, but not from oxaloacetate decarboxylase. 4. The intracellular localization of the NAD-linked ‘malic’ enzyme was predominantly mitochondrial; latency studies suggested a localization in the mitochondrial matrix space. 5. Studies on the partially purified enzyme demonstrated that it had a pH optimum between 7.6 and 7.9. It required Mg2+ or Mn2+ for activity; Ca2+ was not effective. The maximum rate was the same with either cation, but the concentration of Mn2+ required was 100 times less than that of Mg2+. Acitivity with NADP was only 1-3% of that with NAD, unless very high (greater than 10mM) concentrations of Mn2+ were present. 6. It is suggested that the NAD-linked ‘malic’ enzyme functions in the proline-oxidation pathway predominant in tse-tse fly flight muscle.

scholarly journals Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity

FEBS Letters ◽  
2001 ◽  
Vol 493 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Liliana Llanos ◽  
René Briones ◽  
Alejandro Yévenes ◽  
Fernando D González-Nilo ◽  
Perry A Frey ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Decarboxylase Activity ◽  
Oxaloacetate Decarboxylase
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