Document Detail


L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases.
MedLine Citation:
PMID:  10642506     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
L-Pipecolic acid oxidase activity is deficient in patients with peroxisome biogenesis disorders (PBDs). Because its role, if any, in these disorders is unknown, we cloned the associated human gene and expressed its protein product. The cDNA was cloned with the use of a reverse genetics approach based on the amino acid sequence obtained from purified L-pipecolic acid oxidase from monkey. The complete cDNA, obtained by conventional library screening and 5' rapid amplification of cDNA ends, encompassed an open reading frame of 1170 bases, translating to a 390-residue protein. The translated protein terminated with the sequence AHL, a peroxisomal targeting signal 1. Indirect immunofluorescence studies showed that the protein product was expressed in human fibroblasts in a punctate pattern that co-localized with the peroxisomal enzyme catalase. A BLAST search with the amino acid sequence showed 31% identity and 53% similarity with Bacillus sp. NS-129 monomeric sarcosine oxidase, as well as similarity to all sarcosine oxidases and dehydrogenases. No similarity was found to the peroxisomal D-amino acid oxidases. The recombinant enzyme oxidized both L-pipecolic acid and sarcosine. However, PBD patients who lack the enzyme activity accumulate only L-pipecolic acid, suggesting that in humans in vivo, this enzyme is involved mainly in the degradation of L-pipecolic acid.
Authors:
G Dodt; D G Kim; S A Reimann; B E Reuber; K McCabe; S J Gould; S J Mihalik
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  345 Pt 3     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-03-23     Completed Date:  2000-03-23     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  487-94     Citation Subset:  IM    
Affiliation:
Institut für Physiologische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Federal Republic of Germany.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AF134593
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Carrier Proteins / genetics,  metabolism
Cloning, Molecular
Haplorhini
Humans
Kidney / enzymology
Liver / enzymology
Molecular Sequence Data
Oxidoreductases Acting on CH-NH Group Donors / genetics*,  isolation & purification,  metabolism*
Oxidoreductases, N-Demethylating / chemistry,  metabolism
Peroxisomal Disorders / metabolism
Peroxisomes / metabolism
Phylogeny
Pipecolic Acids / blood,  metabolism*
Receptors, Cytoplasmic and Nuclear / metabolism
Recombinant Proteins / genetics,  metabolism
Sarcosine / blood
Sarcosine Oxidase
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Substrate Specificity
Grant Support
ID/Acronym/Agency:
HD10981/HD/NICHD NIH HHS; HD24081/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Pipecolic Acids; 0/Receptors, Cytoplasmic and Nuclear; 0/Recombinant Proteins; 0/maltose-binding protein; 0/peroxisome-targeting signal 1 receptor; 107-97-1/Sarcosine; 535-75-1/pipecolic acid; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.-/Oxidoreductases, N-Demethylating; EC 1.5.3.1/PIPOX protein, human; EC 1.5.3.1/Sarcosine Oxidase; EC 1.5.99.3/L-pipecolate dehydrogenase
Comments/Corrections

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