scholarly journals Reverse Reaction of Malic Enzyme for HCO3−Fixation into Pyruvic Acid to SynthesizeL-Malic Acid with Enzymatic Coenzyme Regeneration

2008 ◽  
Vol 72 (5) ◽  
pp. 1278-1282 ◽  
Author(s):  
Yoko OHNO ◽  
Toshihiko NAKAMORI ◽  
Haitao ZHENG ◽  
Shin-ichiro SUYE
Keyword(s):  
Pyruvic Acid ◽  
Malic Acid ◽  
Malic Enzyme ◽  
Reverse Reaction ◽  
Coenzyme Regeneration

REGULATION OF THE "MALIC" ENZYME IN NEUROSPORA CRASSA

1967 ◽  
Vol 13 (9) ◽  
pp. 1211-1221 ◽  
Author(s):  
M. W. Zink
Keyword(s):  
Cell Growth ◽  
Neurospora Crassa ◽  
Growth Phase ◽  
Pyruvic Acid ◽  
Malic Acid ◽  
Malic Enzyme ◽  
Enzyme Preparation ◽  
Growth Cycle ◽  
Oxidative Decarboxylation ◽  
Enzyme Repression

"Malic" enzyme has been isolated from Neurospora crassa which can bring about the reversible carboxylation of pyruvic acid. The enzyme is specific to L-malate and NADP and is activated by Mn++ and Mg++. The partially purified enzyme does not decarboxylate oxaloacetate but is competitively inhibited by it. This enzyme is synthesized only during the early stages of the growth cycle and is repressed by acetate. In addition, the oxidative decarboxylation of malic acid is competitively inhibited by aspartic acid; the degree of inhibition depends upon the cell growth phase from which the enzyme is extracted. "Malic" enzyme isolated from a 12-h culture is not significantly inhibited by aspartate. However, this inhibition increases to 90% if an enzyme preparation from a 24-h culture is used. The significance of enzyme repression by acetate and the inhibition of the activity by aspartate are discussed.

Intracellular Conversion of Malate and Localization of Enzymes Involved in the Metabolism of Malate in Photoautotrophic Cell Cultures of Chenopodium rubrum

1992 ◽  
Vol 47 (7-8) ◽  
pp. 545-552 ◽  
Author(s):  
Shin-ichi Amino
Keyword(s):  
Subcellular Localization ◽  
Cell Suspension ◽  
Malate Dehydrogenase ◽  
Cell Cultures ◽  
Malic Acid ◽  
Enzyme Activities ◽  
Malic Enzyme ◽  
Mitochondrial Fraction ◽  
Enzymatic Activities ◽  
Chenopodium Rubrum

Cells from photoautotrophic cultures of Chenopodium rubrum were fractionated for the isolation of purified chloroplasts and mitochondria. The subcellular localization of the enzymatic activities involved in the metabolism of malic acid was investigated. Highly purified chloroplasts were obtained from the protoplasts, whereas peroxisomes were still present in the mitochondrial fraction. NAD - and NADP-dependent malate dehydrogenase and malic enzyme activities were found in the mitochondrial and chloroplast fractions, respectively. Exogenously supplied [14C]labelled malate was metabolized by the photoautotrophic cell suspension, obviously to the greater part in mitochondria.

Sign in / Sign up

Export Citation Format

Share Document