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A novel transaminase, (<Emphasis Type="Italic">R</Emphasis>)-amine:pyruvate aminotransferase,from <Emphasis Type="Italic">Arthrobacter</Emphasis> sp. KNK168 (FERM BP-5228): purification,characterization, and gene cloning
Authors:Email author" target="_blank">Akira?IwasakiEmail author  Keiji?Matsumoto  Junzo?Hasegawa  Yoshihiko?Yasohara
Institution:(1) QOL Division Technology Management Department Research Group, Kaneka Corporation, 1-8, Miyamae, Takasago Hyogo, 676-8688, Japan;(2) Frontier Biochemical & Medical Research Laboratories, Kaneka Corporation, 1-8, Miyamae, Takasago Hyogo, 676-8688, Japan
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 ms 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.
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