Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans.
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Chen CD, Huang TF, Lin CH, Guan HH, Hsieh YC, Lin YH, Huang YC, Liu MY, Chang WC, Chen CJ
Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):492-4. Epub 2007 May 5.
- PubMed ID
- 17554170 [ View in PubMed]
- Abstract
The branched-chain amino-acid aminotransferase (BCAT), which requires pyridoxal 5'-phosphate (PLP) as a cofactor, is a key enzyme in the biosynthetic pathway of the hydrophobic amino acids leucine, isoleucine and valine. DrBCAT from Deinococcus radiodurans, which has a molecular weight of 40.9 kDa, was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data to 2.50 A resolution from a DrBCAT crystal, the crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.37, b = 90.70, c = 155.47 A. Preliminary analysis indicates the presence of two DrBCAT molecules in the asymmetric unit, with a solvent content of 47.52%.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Isoleucine Branched-chain-amino-acid aminotransferase, cytosolic Protein Humans UnknownNot Available Details Leucine Branched-chain-amino-acid aminotransferase, cytosolic Protein Humans UnknownNot Available Details Valine Branched-chain-amino-acid aminotransferase, cytosolic Protein Humans UnknownNot Available Details - Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Valine Branched-chain-amino-acid aminotransferase, cytosolic Protein Humans UnknownSubstrateDetails