Document Detail


Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase.
MedLine Citation:
PMID:  11717275     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Pipecolic acid is a component of several secondary metabolites in plants and fungi. This compound is useful as a precursor of nonribosomal peptides with novel pharmacological activities. In Penicillium chrysogenum pipecolic acid is converted into lysine and complements the lysine requirement of three different lysine auxotrophs with mutations in the lys1, lys2, or lys3 genes allowing a slow growth of these auxotrophs. We have isolated two P. chrysogenum mutants, named 7.2 and 10.25, that are unable to convert pipecolic acid into lysine. These mutants lacked, respectively, the pipecolate oxidase that converts pipecolic acid into piperideine-6-carboxylic acid and the saccharopine reductase that catalyzes the transformation of piperideine-6-carboxylic acid into saccharopine. The 10.25 mutant was unable to grow in Czapek medium supplemented with alpha-aminoadipic acid. A DNA fragment complementing the 10.25 mutation has been cloned; sequence analysis of the cloned gene (named lys7) revealed that it encoded a protein with high similarity to the saccharopine reductase from Neurospora crassa, Magnaporthe grisea, Saccharomyces cerevisiae, and Schizosaccharomyces pombe. Complementation of the 10.25 mutant with the cloned gene restored saccharopine reductase activity, confirming that lys7 encodes a functional saccharopine reductase. Our data suggest that in P. chrysogenum the conversion of pipecolic acid into lysine proceeds through the transformation of pipecolic acid into piperideine-6-carboxylic acid, saccharopine, and lysine by the consecutive action of pipecolate oxidase, saccharopine reductase, and saccharopine dehydrogenase.
Authors:
L Naranjo; E Martin de Valmaseda; O Bañuelos; P Lopez; J Riaño; J Casqueiro; J F Martin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  183     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2001 Dec 
Date Detail:
Created Date:  2001-11-21     Completed Date:  2001-12-26     Revised Date:  2013-04-17    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7165-72     Citation Subset:  IM    
Affiliation:
Area of Microbiology, Faculty of Biology and Environmental Sciences, University of León, León, Spain.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AJ319030
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Cloning, Molecular
Genes, Fungal
Genetic Complementation Test
Lysine / biosynthesis*
Molecular Sequence Data
Mutation
Open Reading Frames
Oxidoreductases Acting on CH-NH Group Donors / metabolism
Penicillium chrysogenum / genetics*,  metabolism
Pipecolic Acids / metabolism*
Plasmids
Saccharopine Dehydrogenases / genetics*,  metabolism
Sequence Homology, Amino Acid
Transformation, Bacterial
Chemical
Reg. No./Substance:
0/Pipecolic Acids; 535-75-1/pipecolic acid; 56-87-1/Lysine; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.1.-/Saccharopine Dehydrogenases; EC 1.5.1.10/saccharopine dehydrogenase (NADP, L-glutamate-forming); EC 1.5.1.8/saccharopine dehydrogenase (NADP+, lysine-forming); EC 1.5.99.3/L-pipecolate dehydrogenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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