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1998 Fiscal Year Final Research Report Summary

Enzymological and molecular analysis of a novel multiple-substrate aminotransferase from a hyperthermophilic archaeon.

Research Project

Project/Area Number 09660077
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 応用微生物学・応用生物化学
Research InstitutionNagoya University

Principal Investigator

KOBAYASHI Tetsuo  Nagoya Univ., Agriculture, Associate Professor, 農学部, 助教授 (20170334)

Project Period (FY) 1997 – 1998
Keywordshyperthermophile / Thermococcus profundus / aminotransferase / クローニング
Research Abstract

A hyperthermophilic archaeon, Thermococcus profundus, possessed an amino acid aminotransferase with extremely broad substrate specificity (multiple-substrate aminotransferase ; MsAT). MsAT was composed of two homogeneous subunits of 45,000. The maximal activity was detected at above 80゚C and between pH 6.0 and 8.0. Pyridoxal 5'-phosphate was required for the activity. The enzyme catalyzed aminotransfer from L-alanine, L-leucine, L-isoleucine, L-valine, L-phenylalanine, L-tyrosine, L-tryptophan, L-methionine, L-cystein, L-threonine and L-lysine using 2-oxoglutarate as an amino receptor.
The gene encoding MsAT was cloned and expressed in Escherichia coil. MsAT revealed only a low degree of sequence identity (less than 25%) to any aminotransferases so far characterized. However, homology search against EMBL database revealed that Pyrococcus horikoshii and Sulfolobus solfataricus possessed an open reading frame homologous to the MsAT gene. MsAT and these homologues formed a novel cluster independent from other aminotransferases on an evolutionary tree based on the amino acid sequences.

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Published: 1999-12-08  

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