PMID- 10464321
OWN - NLM
STAT- MEDLINE
DCOM- 19991007
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 36
DP  - 1999 Sep 3
TI  - The mouse gene PDCR encodes a peroxisomal delta(2), delta(4)-dienoyl-CoA
      reductase.
PG  - 25814-20
AB  - Here we describe the identification and characterization of a novel mouse gene,
      PDCR, that encodes a peroxisomal Delta(2), Delta(4)-dienoyl-CoA reductase. The
      mouse PDCR cDNA contains an 892-base pair open reading frame and is predicted to 
      encode a 292-amino acid protein with a deduced molecular mass of 31,298 Da that
      terminates in a consensus type-1 peroxisomal targeting signal. Purified
      recombinant PDCR protein was generated from Escherichia coli and catalyzed the
      NADPH-dependent reduction of Delta(2)-trans, Delta(4)-trans-decadienoyl-CoA with 
      a specific activity of 20 units/mg. Enzymatic characterization followed by high
      pressure liquid chromatography analysis of the products revealed that PDCR
      converted Delta(2)-trans,Delta(4)-trans-decadienoyl-CoA to a Delta(3)-enoyl-CoA
      but not to a Delta(2)-enoyl-CoA. Kinetic analyses demonstrated that PDCR is
      active on a broad range of Delta(2), Delta(4)-dienoyl-CoAs. Although the observed
      substrate preference was to Delta(2)-trans,Delta(4)-trans-decadienoyl-CoA, PDCR
      was also active on a C(22) substrate with multiple unsaturations, a result
      consistent with the role of peroxisomes in the oxidation of complex, very long
      chain, polyunsaturated fatty acids. The presence of a type-1 peroxisomal
      targeting signal Ala-Lys-Leu-COOH at the C terminus of PDCR suggested that this
      protein may be peroxisomal. We observed that tagged PDCR was efficiently
      transported to the peroxisome lumen in normal human fibroblasts but not in cells 
      derived from a Zellweger syndrome patient with a specific defect in peroxisomal
      matrix protein import. We conclude that this protein resides within the
      peroxisome matrix and therefore represents the first mammalian peroxisomal
      Delta(2),Delta(4)-dienoyl-CoA reductase to be characterized at the molecular
      level.
FAU - Geisbrecht, B V
AU  - Geisbrecht BV
AD  - Department of Biological Chemistry, The Johns Hopkins University School of
      Medicine, Baltimore, Maryland 21205, USA.
FAU - Liang, X
AU  - Liang X
FAU - Morrell, J C
AU  - Morrell JC
FAU - Schulz, H
AU  - Schulz H
FAU - Gould, S J
AU  - Gould SJ
LA  - eng
GR  - DK45787/DK/NIDDK NIH HHS/United States
GR  - HD10981/HD/NICHD NIH HHS/United States
GR  - HL30847/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 1.14.19.- (Fatty Acid Desaturases)
RN  - EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors)
RN  - EC 1.3.1.34 (2,4-dienoyl-CoA reductase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Fatty Acid Desaturases/*genetics/metabolism
MH  - Genome
MH  - Humans
MH  - Mice
MH  - Microbodies/*enzymology
MH  - Molecular Sequence Data
MH  - *Oxidoreductases Acting on CH-CH Group Donors
MH  - Sequence Alignment
EDAT- 1999/08/28 00:00
MHDA- 1999/08/28 00:01
CRDT- 1999/08/28 00:00
PHST- 1999/08/28 00:00 [pubmed]
PHST- 1999/08/28 00:01 [medline]
PHST- 1999/08/28 00:00 [entrez]
AID - 10.1074/jbc.274.36.25814 [doi]
AID - S0021-9258(19)55345-5 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 3;274(36):25814-20. doi: 10.1074/jbc.274.36.25814.