Cloning and Characterization of pcd Encoding Δ'-Piperideine-6-Carboxylate Dehydrogenase from Flavobacterium lutescens IFO3084

The pcd gene from Flavobacterium lutescens IFO3084 encoding Δ'-piperideine-6-carbox-ylate 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 clavuligeru...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 2000-12, Vol.128 (6), p.975-982
Main Authors: Fujii, Tadashi, Narita, Takao, Agematu, Hitosi, Agata, Naoki, Isshiki, Kunio
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins
Base Sequence
Cloning, Molecular
DNA, Bacterial
Flavobacterium - enzymology
Flavobacterium lutescens IFO3084
l-α-aminoadipic acid (l-AAA)
lat
Molecular Sequence Data
Oxidoreductases Acting on CH-NH Group Donors - chemistry
Oxidoreductases Acting on CH-NH Group Donors - genetics
Oxidoreductases Acting on CH-NH Group Donors - metabolism
pcd
Sequence Homology, Amino Acid
Δ'-piperideine-6-carboxylate (P6C)
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Summary:The pcd gene from Flavobacterium lutescens IFO3084 encoding Δ'-piperideine-6-carbox-ylate 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-α-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.
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a022849