Abstract:
:The pcd gene from Flavobacterium lutescens IFO3084 encoding Delta'-piperideine-6-carboxylate dehydrogenase (PCD) was cloned, sequenced, and expressed in Escherichia coli. The deduced amino acid sequence of PCD from F. lutescens IFO3084 showed strong similarity to that from Streptomyces clavuligerus. The molecular mass of the recombinant PCD was estimated to be approximately 58,000 Da by SDS-PAGE and native PAGE, which indicated that the enzyme molecule is a monomer. The in vitro analysis of L-alpha-aminoadipic acid (L-AAA) production showed that L-AAA is synthesized from L-lysine in two steps catalyzed by L-lysine 6-aminotransferase (LAT) and PCD from F. lutescens IFO3084.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Fujii T,Narita T,Agematu H,Agata N,Isshiki Kdoi
10.1093/oxfordjournals.jbchem.a022849keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
975-82issue
6eissn
0021-924Xissn
1756-2651journal_volume
128pub_type
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更新日期:2010-01-01 00:00:00
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