Entry - *605843 - PEROXISOMAL TRANS-2-ENOYL-CoA REDUCTASE; PECR - OMIM
 
* 605843

PEROXISOMAL TRANS-2-ENOYL-CoA REDUCTASE; PECR


Alternative titles; symbols

TRANS-2-ENOYL-CoA REDUCTASE, PEROXISOMAL; TERP


HGNC Approved Gene Symbol: PECR

Cytogenetic location: 2q35   Genomic coordinates (GRCh38) : 2:216,029,088-216,081,809 (from NCBI)


TEXT

Cloning and Expression

Chain elongation of fatty acids occurs in endoplasmic reticulum (ER) and mitochondria and is thought to occur in peroxisomes. Like the mitochondrial system, the proposed peroxisomal system requires a 2-enoyl-CoA reductase for the last step of elongation. During purification of acyl-DHAP reductase from guinea pig liver peroxisomes, Das et al. (2000) identified trans-2-enoyl-CoA reductase, which they partially purified by affinity chromatography. By searching EST databases and screening cDNA libraries, they identified cDNAs encoding trans-2-enoyl-CoA reductase in guinea pig, mouse, and human. The deduced human protein contains 303 amino acids, including a C-terminal type I peroxisomal targeting signal (AKL), and has a predicted molecular mass of 33 kD. The guinea pig, mouse, and human proteins share 71 to 75% amino acid identity. Northern blot analysis of mouse tissues detected a 1.3-kb transcript expressed at high levels in liver and kidney, with lower levels in heart, skeletal muscle, and other tissues. Using transformed cells expressing a tagged recombinant guinea pig or human protein, Das et al. (2000) demonstrated that the protein has high NADPH-specific 2-enoyl-CoA reductase activity. The enzyme was found to catalyze the reduction of trans-2-enoyl-CoAs of varying chain lengths. Western blot analysis of guinea pig liver subcellular fractions demonstrated that the protein is a peroxisomal enzyme. Das et al. (2000) hypothesized that this NADPH-specific trans-2-enoyl-CoA reductase is the key enzyme for the proposed peroxisomal chain elongation pathway.


Mapping

Scott (2001) mapped the peroxisomal trans-2-enoyl-CoA reductase gene (PECR) to chromosome 2 based on sequence similarity between the peroxisomal trans-2-enoyl-CoA reductase sequence (GenBank AF119841) and a chromosome 2 clone (GenBank AC010606).


REFERENCES

  1. Das, A. K., Uhler, M. D., Hajra, A. K. Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J. Biol. Chem. 275: 24333-24340, 2000. [PubMed: 10811639, related citations] [Full Text]

  2. Scott, A. F. Personal Communication. Baltimore, Md. 4/12/2001.


Creation Date:
Dawn Watkins-Chow : 4/12/2001
alopez : 09/12/2005
mgross : 8/28/2001
mgross : 4/12/2001

* 605843

PEROXISOMAL TRANS-2-ENOYL-CoA REDUCTASE; PECR


Alternative titles; symbols

TRANS-2-ENOYL-CoA REDUCTASE, PEROXISOMAL; TERP


HGNC Approved Gene Symbol: PECR

Cytogenetic location: 2q35   Genomic coordinates (GRCh38) : 2:216,029,088-216,081,809 (from NCBI)


TEXT

Cloning and Expression

Chain elongation of fatty acids occurs in endoplasmic reticulum (ER) and mitochondria and is thought to occur in peroxisomes. Like the mitochondrial system, the proposed peroxisomal system requires a 2-enoyl-CoA reductase for the last step of elongation. During purification of acyl-DHAP reductase from guinea pig liver peroxisomes, Das et al. (2000) identified trans-2-enoyl-CoA reductase, which they partially purified by affinity chromatography. By searching EST databases and screening cDNA libraries, they identified cDNAs encoding trans-2-enoyl-CoA reductase in guinea pig, mouse, and human. The deduced human protein contains 303 amino acids, including a C-terminal type I peroxisomal targeting signal (AKL), and has a predicted molecular mass of 33 kD. The guinea pig, mouse, and human proteins share 71 to 75% amino acid identity. Northern blot analysis of mouse tissues detected a 1.3-kb transcript expressed at high levels in liver and kidney, with lower levels in heart, skeletal muscle, and other tissues. Using transformed cells expressing a tagged recombinant guinea pig or human protein, Das et al. (2000) demonstrated that the protein has high NADPH-specific 2-enoyl-CoA reductase activity. The enzyme was found to catalyze the reduction of trans-2-enoyl-CoAs of varying chain lengths. Western blot analysis of guinea pig liver subcellular fractions demonstrated that the protein is a peroxisomal enzyme. Das et al. (2000) hypothesized that this NADPH-specific trans-2-enoyl-CoA reductase is the key enzyme for the proposed peroxisomal chain elongation pathway.


Mapping

Scott (2001) mapped the peroxisomal trans-2-enoyl-CoA reductase gene (PECR) to chromosome 2 based on sequence similarity between the peroxisomal trans-2-enoyl-CoA reductase sequence (GenBank AF119841) and a chromosome 2 clone (GenBank AC010606).


REFERENCES

  1. Das, A. K., Uhler, M. D., Hajra, A. K. Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J. Biol. Chem. 275: 24333-24340, 2000. [PubMed: 10811639] [Full Text: https://doi.org/10.1074/jbc.M001168200]

  2. Scott, A. F. Personal Communication. Baltimore, Md. 4/12/2001.


Creation Date:
Dawn Watkins-Chow : 4/12/2001

Edit History:
alopez : 09/12/2005
mgross : 8/28/2001
mgross : 4/12/2001