Activities | Families | Sequences | Fold types | References | Help
B6db references: 14680702.

type Journal Article
authors Vernal, J.; Cazzulo, J.; Nowicki, C.
title Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes1
journal FEMS Microbiol Lett
sel selected
ui 14680702
year (2003)
volume 229
number 2
pages 217-22
keywords Amino Acid Sequence
abstract We have previously reported that Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing in Escherichia coli the recombinant active protein. The amino acid sequence of BSAT shares over 40% identity with other eukaryotic and prokaryotic aspartate aminotransferases, thus showing that the enzyme belongs to the subfamily Ialpha of aminotransferases, and has only 6% identity with the tyrosine aminotransferase from Trypanosoma cruzi, which has a similar substrate specificity. The production of recombinant active enzyme in good yields opens up the possibility of obtaining its 3D-structure, in order to investigate the structural basis of the broad substrate specificity.
last changed 2017/09/14 09:01

B6db references