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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 29, Number 1
BKCSDE 29(1)
January 20, 2008 

Crystal Structure of MJ0684 from Methanococcus jannaschii,
a Novel Archaeal Homolog of Kynurenine Aminotransferase
Jin Kuk Yang
Amino acid aminotransferase, Kynurenine aminotransferase, MJ0684
MJ0684 from Methanococcus jannaschii is a hypothetical protein belonging to the subfamily Iγ of amino acid aminotransferases. In the present study, the crystal structure of MJ0684 has been determined at 2.2 A resolution. It reveals that MJ0684 has an overall structure similar to subfamily Iγ aminotransferases and its active site architecture is most similar to that of kynurenine aminotransferases among several kinds of aminotransferases in the subfamily Iγ . It has two hydrophobic active site residues conserved in the kynurenine aminotransferases for recognizing hydrophobic substrates. In addition, the absence of any basic residue for recognizing the side chain carboxylic group of the aspartate in the active site rules out the possibility that MJ0684 would act as an aspartate aminotransferase. These structural observations collectively imply that MJ0684 is a novel archaeal homolog of the subfamily Iγ kynurenine aminotransferase.
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