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Comparative studies of NADP-malic enzyme from C4- and C3-plants
Biochemical and Biophysical Research Communications, 1974Abstract Some enzymological properties were studied comparatively for NADP-malic enzyme from various C 4 - and C 3 -plants. The enzyme from C 4 -plants of “malate formers” showed relatively low Km(Mal) values (0.10 – 0.25 mM) and high pH optima (more than pH 7.4 – 7.8).
T, Nishikido, T, Wada
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Analogues of NADP+ as inhibitors and coenzymes for NADP+ malic enzyme from maize leaves
Photosynthesis Research, 1991Structural analogues of the NADP(+) were studied as potential coenzymes and inhibitors for NADP(+) dependent malic enzyme from Zea mays L. leaves. Results showed that 1, N(6)-etheno-nicotinamide adenine dinucleotide phosphate (∈ NADP(+)), 3-acetylpyridine-adenine dinucleotide phosphate (APADP(+)), nicotinamide-hypoxanthine dinucleotide phosphate (NHDP(+
C P, Spampinato +3 more
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Study of the Structure Function Relationship in Maize NADP—Malic Enzyme
2008NADP-malic enzyme catalyses the reversible oxidative decarboxylation of l-malate to yield carbon dioxide and pyruvate with the concomitant reduction of NADP. Maize presents at least three isoforms of this enzyme, and the “photosynthetic isoform” is responsible for providing CO2 to the Calvin Cycle for carbon fixation. In this work, different aspects of
Enrique Detarsio +4 more
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A comparative study of the NADP-malic enzymes from Drosophila and chick liver
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1980Abstract 1. 1. NADP-Malic enzyme (NADP-ME; l -malate:NADP + oxidoreductase (decarboxylating) EC 1.1.1.40) from Drosophila melanogaster has a mol wt of 266,000 and a subunit mol wt of 67,250 ± 3080. The amino acid composition of Drosophila NADP-ME is closely related to the NADP-ME's from pigeon liver, chick liver, rat liver and E.
B.W. Geer +4 more
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Presence of essential histidine residues in nadp-malic enzyme from maize
Phytochemistry, 1987Abstract Modification of maize leaf NADP-malic enzyme by diethylpyrocarbonate (DEP) caused rapid and complete inactivation of the enzyme. The inactivation followed pseudo-first-order reaction kinetics. The inactivation of the enzyme showed saturation kinetics with a half inactivation time, at saturating DEP, equal to 0.15 min and KDEP = 20 mM.
Narendra Jawali, Anil S. Bhagwat
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A study on the inactivation of maize leaves nadp-malic enzyme by 3-bromopyruvate
Phytochemistry, 1992Abstract Bromopyruvate is a noncompetitive inhibitor of maize leaf NADP + -malic enzyme with respect to l -Malate ( K i 1 mM at pH 8.0). Relatively low concentrations of this compound completely and irreversibly inactivated the enzyme. The inactivation followed pseudo-first-order kinetics.
Maria F. Drincovich, Carlos S. Andreo
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NADP-malic enzyme from maize leaves: a fluorescence study.
Biochemistry and molecular biology international, 1996NADP-malic enzyme from maize leaves is covalently labeled with a fluorescent-SH reactive probe eosin-5-maleimide (EMA), which reacts with groups that are totally protected by NADP against inactivation. The comparison of the emission fluorescence spectra of the native and the modified enzyme suggests the proximity of the fluorescent groups of the native
M F, Drincovich, C S, Andreo
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Evolution of C4 photosynthesis in flaveria species. Isoforms Of nadp-malic enzyme
Plant physiologyNADP-malic enzyme (NADP-ME, EC 1.1.1.40), a key enzyme in C4 photosynthesis, provides CO2 to the bundle-sheath chloroplasts, where it is fixed by ribulose-1,5-bisphosphate carboxylase/oxygenase. We characterized the isoform pattern of NADP-ME in different photosynthetic species of Flaveria (C3, C3-C4 intermediate, C4-like, C4) based on sucrose density ...
, Drincovich +6 more
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An intermediate form of NADP-malic enzyme from the C3 C4 intermediate species Flaveria floridana
Plant Science, 1999Paula Casati, CARLOS S Andreo
exaly