type	Journal Article
authors	Iwasaki A, Matsumoto K, Hasegawa J, Yasohara Y.
title	A novel transaminase, (R)-amine:pyruvate aminotransferase, from Arthrobacter sp. KNK168 (FERM BP-5228): purification, characterization, and gene cloning.
journal	Appl Microbiol Biotechnol.
Activity	r-amine.pyruvate.aminotransferase
Family	r-amine.pyruvate.aminotransferase
sel	selected
ui	22002066
year	(2012)
volume	93
number	4
pages	1563-73
abstract	A novel (R)-amine transaminase, which catalyzed (R)-enantioselective transamination of chiral amine, was purified to homogeneity from Arthrobacter sp. KNK168 (FERM BP-5228). The molecular mass of the enzyme was estimated to be 148 kDa by gel filtration and 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis, suggesting a homotetrameric structure. The enzyme catalyzed transamination between amines and pyruvate stereo-specifically. The reaction on 1-methylbenzylamine was (R)-enantioselective. Pyruvate was the best amino acceptor, but the enzyme showed broad amino acceptor specificity for various ketone and aldehyde compounds. The apparent K(m)s for (R)-1-methylbenzylamine and pyruvate were 2.62 and 2.29 mM, respectively. The cloned gene of the enzyme consists of an open reading frame (ORF) of 993 bp encoding a protein of 330 amino acids, with a calculated molecular weight of 36,288. The deduced amino acid sequence was found to be homologous to those of the aminotransferases belonging to fold class IV of pyridoxal-5'-phosphate-dependent enzymes, such as branched-chain amino acid aminotransferases.
last changed	2014/04/16 13:39