FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties.
FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme, was homogeneously purified from the particulate fraction of Mycobacterium sp. strain Takeo. The isolated enzyme contains no FAD and few phospholipid, and has a specific activity of 300-360 units/mg of protein. In the assay system without addition of phospholipid (cardiolipin), the enzyme activity was only about 3% of maximum activity. The molecular weight was estimated to be 51 000-55 000 by four methods. Titration by p-chloromercuribenzoate revealed the presence of one cysteine residue/mol of enzyme. The isoelectric point was found to be pH 6.9 by isoelectric focusing. From circular dichroism spectral data, the enzyme protein was found to contain alpha-helix structure of 24%.
D000596:Amino Acids / Q000032:analysis; D002308:Cardiolipins / Q000494:pharmacology*; D002942:Circular Dichroism; D004789:Enzyme Activation / Q000187:drug effects; D005182:Flavin-Adenine Dinucleotide; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology*; D010743:Phospholipids / Q000494:pharmacology*; D011487:Protein Conformation
D000596:Amino Acids; D002308:Cardiolipins; D010743:Phospholipids; D005182:Flavin-Adenine Dinucleotide; D008291:Malate Dehydrogenase