Visible light and enzymatic induced synthesis of malic acid from pyruvic acid and HCO3- with the combination system of zinc chlorophyll derivative and malic enzyme in water media

2007 ◽  
Vol 8 (3) ◽  
pp. 523-526 ◽  
Author(s):  
Yutaka Amao ◽  
Mitsue Ishikawa
Keyword(s):  
Visible Light ◽  
Pyruvic Acid ◽  
Malic Acid ◽  
Malic Enzyme ◽  
Chlorophyll Derivative ◽  
Combination System ◽  
Water Media

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.

Development of a dye molecule-biocatalyst hybrid system with visible-light induced carbon–carbon bond formation from CO2 as a feedstock

2017 ◽  
Vol 198 ◽  
pp. 73-81 ◽  
Author(s):  
Yutaka Amao ◽  
Shusaku Ikeyama ◽  
Takayuki Katagiri ◽  
Kohei Fujita
Keyword(s):  
Visible Light ◽  
Electron Donor ◽  
Pyruvic Acid ◽  
Malic Acid ◽  
Bond Formation ◽  
Major Product ◽  
Water Soluble ◽  
Electron Mediator ◽  
Carbon Bond ◽  
Carbon Carbon Bond

Recently, CO2 utilization technology, including artificial photosynthesis, has received much attention. In this field, CO2 is used as a feedstock for fuels, polymers and in other chemical processes. Of note are malic enzymes (MEs) which catalyze the reaction of malic acid to pyruvic acid and CO2 with the co-enzyme NADP+, and catalyze the reverse reaction of pyruvic acid and CO2 to malic acid with the co-enzyme NADPH. Thus, MEs are also an attractive biocatalyst for carbon–carbon bond formation from CO2. Studies of the visible light-induced malic acid production from pyruvic acid and CO2 using an electron donor, a photosensitizer, an electron mediator, ferredoxin-NADP+ reductase, NADP+, and ME have been reported. However, modification of these systems is required, as they are very complicated. In this study, the visible light-induced carbon–carbon bond formation from pyruvic acid and CO2 with ME using the photoreduction of 1,1′-diphenyl-4,4′-bipyridinium salt derivatives as a novel electron mediator with water-soluble tetraphenylporphyrin tetrasulfonate (H2TPPS) in the presence of triethanolamine (TEOA) as an electron donor was developed. When a sample solution containing TEOA, H2TPPS, 1,1′-diphenyl-4,4′-bipyridinium salt derivative, pyruvic acid, and ME in CO2-saturated bis–tris buffer was irradiated, the major product was oxaloacetic acid. Thus, a visible light-induced photoredox system for carbon–carbon bond formation from CO2 with ME using 1,1′-diphenyl-4,4′-bipyridinium salt derivative as an electron mediator was developed.

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.

scholarly journals Contaminant of malic acid: A malic enzyme inhibitor

FEBS Letters ◽  
1971 ◽  
Vol 14 (5) ◽  
pp. 283-284 ◽  
Author(s):  
D.B. Anderson ◽  
S.M.F. Ferguson ◽  
H.A. Lardy
Keyword(s):  
Malic Acid ◽  
Malic Enzyme ◽  
Enzyme Inhibitor
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