Cloning and characterization of pcd encoding delta'-piperideine-6-carboxylate dehydrogenase from flavobacterium lutescens IFO3084.

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 Biochem

journal_title

Journal of biochemistry

authors

Fujii T,Narita T,Agematu H,Agata N,Isshiki K

doi

10.1093/oxfordjournals.jbchem.a022849

keywords:

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

975-82

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

128

pub_type

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