|
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 |
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