Mitochondrial malic enzymes. Purification and properties of the NAD(P)-dependent malic enzyme from canine small intestinal mucosa.
نویسندگان
چکیده
منابع مشابه
Purification, cDNA cloning and heterologous expression of the human mitochondrial NADP(+)-dependent malic enzyme.
Mitochondrial NADP(+)-dependent malic enzyme (ME; EC 1.1.1.39) has been purified to homogeneity and characterized kinetically from bovine heart. Partial amino acid sequence information allowed amplification of a specific bovine cDNA, which was used to isolate a full-length human cDNA of this isoform of ME. The cDNA is 1930 bp long and codes for a protein of 604 amino acids. Comparison of the am...
متن کاملStructural studies of the pigeon cytosolic NADP(+)-dependent malic enzyme.
Malic enzymes are widely distributed in nature, and have important biological functions. They catalyze the oxidative decarboxylation of malate to produce pyruvate and CO(2) in the presence of divalent cations (Mg(2+), Mn(2+)). Most malic enzymes have a clear selectivity for the dinucleotide cofactor, being able to use either NAD(+) or NADP(+), but not both. Structural studies of the human mitoc...
متن کاملPrimary structure of the maize NADP-dependent malic enzyme.
Chloroplast-localized NADP-dependent malic enzyme (EC 1.1.1.40) (NADP-ME) provides a key activity for the carbon 4 fixation pathway. In maize, nuclear encoded NADP-ME is synthesized in the cytoplasm as a precursor with a transit peptide that is removed upon transport into the chloroplast stroma. We present here the complete nucleotide sequence for a 2184-base pair full-length maize NADP-ME cDNA...
متن کاملLimited proteolysis of maize NADP-malic enzyme.
The incubation of maize malic enzyme at 37 degrees C with trypsin at a ratio of 150:1 of malic enzyme to trypsin caused rapid and complete inactivation of enzyme activity. The inactivation was caused by fairly specific cleavage of the enzyme monomer (62 kDa) into 40 kDa and 20 kDa fragments. The intensity of 40 kDa band increased with the time of treatment of enzyme with trypsin from 2 to 30 mi...
متن کاملPurification and characterization of the NADP-malic enzyme from Bradyrhizobium japonicum A1017.
An NADP-malic enzyme [EC 1.1.1.40] was purified to homogeneity from Bradyrhizobium japonicum A1017, and the molecular and physiological characteristics were surveyed. The molecular mass of one subunit of the purified enzyme was evaluated to be 77,600 Da by SDS-PAGE, and the native enzyme was a tetramer in pH 7.0 and dimer in pH 8.0 conditions, showing complex oligomeric characteristics correspo...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)33728-1