PMID- 10419495
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 31
DP  - 1999 Jul 30
TI  - Characterization of PECI, a novel monofunctional Delta(3), Delta(2)-enoyl-CoA
      isomerase of mammalian peroxisomes.
PG  - 21797-803
AB  - We report here the identification and characterization of human and mouse PECI, a
      novel gene that encodes a monofunctional peroxisomal Delta(3),Delta(2)-enoyl-CoA 
      isomerase. Human and mouse PECI were identified on the basis of their sequence
      similarity to Eci1p, a recently characterized peroxisomal
      Delta(3),Delta(2)-enoyl-CoA isomerase from the yeast Saccharomyces cerevisiae.
      Cloning and sequencing of the human PECI cDNA revealed the presence of a
      1077-base pair open reading frame predicted to encode a 359-amino acid protein
      with a mass of 39.6 kDa. The corresponding mouse cDNA contains a 1074-base pair
      open reading frame that encodes a 358-amino acid-long protein with a deduced mass
      of 39.4 kDa. Northern blot analysis demonstrated human PECI mRNA is expressed in 
      all tissues. A bacterially expressed form of human PECI catalyzed the
      isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific
      activity of 27 units/mg of protein. The human and mouse PECI proteins contain
      type-1 peroxisomal targeting signals, and human PECI was localized to peroxisomes
      by both subcellular fractionation and immunofluorescence microscopy techniques.
      The potential roles for this monofunctional Delta(3),Delta(2)-enoyl-CoA isomerase
      in peroxisomal metabolism are discussed.
FAU - Geisbrecht, B V
AU  - Geisbrecht BV
AD  - Department of Biological Chemistry, The Johns Hopkins University School of
      Medicine, Baltimore, Maryland 21205, USA.
FAU - Zhang, D
AU  - Zhang D
FAU - Schulz, H
AU  - Schulz H
FAU - Gould, S J
AU  - Gould SJ
LA  - eng
SI  - GENBANK/AA188052
GR  - DK45787/DK/NIDDK NIH HHS/United States
GR  - HD10981/HD/NICHD NIH HHS/United States
GR  - HL30847/HL/NHLBI NIH HHS/United States
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  - 0 (Recombinant Proteins)
RN  - EC 5.3.3.- (Carbon-Carbon Double Bond Isomerases)
RN  - EC 5.3.3.8 (Dodecenoyl-CoA Isomerase)
RN  - EC 5.3.3.8 (ECI1 protein, human)
RN  - EC 5.3.3.8 (ECI2 protein, human)
RN  - EC 5.3.3.8 (Eci1 protein, mouse)
RN  - EC 5.3.3.8 (Eci2 protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carbon-Carbon Double Bond Isomerases/*chemistry/*genetics/metabolism
MH  - Carcinoma, Hepatocellular
MH  - Cells, Cultured
MH  - Cloning, Molecular
MH  - Dodecenoyl-CoA Isomerase
MH  - Escherichia coli
MH  - Fibroblasts/enzymology
MH  - Genes
MH  - Humans
MH  - Kinetics
MH  - Liver Neoplasms
MH  - Mammals
MH  - Mice
MH  - Microbodies/*enzymology
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Polymerase Chain Reaction
MH  - Protein Biosynthesis
MH  - Recombinant Proteins/chemistry/isolation & purification/metabolism
MH  - Saccharomyces cerevisiae/enzymology
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Skin/enzymology
MH  - Tumor Cells, Cultured
EDAT- 1999/07/27 00:00
MHDA- 1999/07/27 00:01
CRDT- 1999/07/27 00:00
PHST- 1999/07/27 00:00 [pubmed]
PHST- 1999/07/27 00:01 [medline]
PHST- 1999/07/27 00:00 [entrez]
AID - 10.1074/jbc.274.31.21797 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 30;274(31):21797-803. doi: 10.1074/jbc.274.31.21797.