PMID- 10642506
OWN - NLM
STAT- MEDLINE
DCOM- 20000323
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 345 Pt 3
DP  - 2000 Feb 1
TI  - L-Pipecolic acid oxidase, a human enzyme essential for the degradation of
      L-pipecolic acid, is most similar to the monomeric sarcosine oxidases.
PG  - 487-94
AB  - 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.
FAU - Dodt, G
AU  - Dodt G
AD  - Institut fur Physiologische Chemie, Ruhr-Universitat Bochum, 44780 Bochum,
      Federal Republic of Germany.
FAU - Kim, D G
AU  - Kim DG
FAU - Reimann, S A
AU  - Reimann SA
FAU - Reuber, B E
AU  - Reuber BE
FAU - McCabe, K
AU  - McCabe K
FAU - Gould, S J
AU  - Gould SJ
FAU - Mihalik, S J
AU  - Mihalik SJ
LA  - eng
SI  - GENBANK/AF134593
GR  - HD10981/HD/NICHD NIH HHS/United States
GR  - HD24081/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Carrier Proteins)
RN  - 0 (Maltose-Binding Proteins)
RN  - 0 (Peroxisome-Targeting Signal 1 Receptor)
RN  - 0 (Pipecolic Acids)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Recombinant Proteins)
RN  - EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
RN  - EC 1.5.- (Oxidoreductases, N-Demethylating)
RN  - EC 1.5.3.1 (PIPOX protein, human)
RN  - EC 1.5.3.1 (Sarcosine Oxidase)
RN  - EC 1.5.99.3 (L-pipecolate dehydrogenase)
RN  - H254GW7PVV (pipecolic acid)
RN  - Z711V88R5F (Sarcosine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carrier Proteins/genetics/metabolism
MH  - Cloning, Molecular
MH  - Haplorhini
MH  - Humans
MH  - Kidney/enzymology
MH  - Liver/enzymology
MH  - Maltose-Binding Proteins
MH  - Molecular Sequence Data
MH  - Oxidoreductases Acting on CH-NH Group Donors/*genetics/isolation &
      purification/*metabolism
MH  - Oxidoreductases, N-Demethylating/chemistry/metabolism
MH  - Peroxisomal Disorders/metabolism
MH  - Peroxisome-Targeting Signal 1 Receptor
MH  - Peroxisomes/metabolism
MH  - Phylogeny
MH  - Pipecolic Acids/blood/*metabolism
MH  - Receptors, Cytoplasmic and Nuclear/metabolism
MH  - Recombinant Proteins/genetics/metabolism
MH  - Sarcosine/blood
MH  - Sarcosine Oxidase
MH  - Sequence Analysis, Protein
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
PMC - PMC1220782
EDAT- 2000/01/22 09:00
MHDA- 2000/03/25 09:00
CRDT- 2000/01/22 09:00
PHST- 2000/01/22 09:00 [pubmed]
PHST- 2000/03/25 09:00 [medline]
PHST- 2000/01/22 09:00 [entrez]
PST - ppublish
SO  - Biochem J. 2000 Feb 1;345 Pt 3:487-94.