fbpx
Wikipedia

MCAT (gene)

Malonyl CoA-acyl carrier protein transacylase, mitochondrial is an enzyme that in humans is encoded by the MCAT gene.[5][6]

MCAT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMCAT, FASN2C, MCT, MT, NET62, fabD, malonyl-CoA-acyl carrier protein transacylase, MCT1
External IDsOMIM: 614479; MGI: 2388651; HomoloGene: 15511; GeneCards: MCAT; OMA:MCAT - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_014507
NM_173467

NM_001030014

RefSeq (protein)

NP_055322
NP_775738

NP_001025185

Location (UCSC)Chr 22: 43.13 – 43.14 MbChr 15: 83.43 – 83.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

The protein encoded by this gene is found exclusively in the mitochondrion, where it catalyzes the transfer of a malonyl group from malonyl-CoA to the mitochondrial acyl carrier protein. The encoded protein may be part of a fatty acid synthase complex that is more like the type II prokaryotic and plastid complexes rather than the type I human cytosolic complex. Two transcript variants encoding different isoforms have been found for this gene.[6]

Clinical significance edit

The enzyme encoded by the MCAT gene, along with other enzymes that regulate Malonyl-CoA concentration, have been shown to regulate levels such that malonyl-CoA concentration decreases in human muscle tissue when under exercise training. This enzyme specifically has increased activity under these conditions, as it is known to catabolize malonyl-CoA. [7]

Interactions edit

The human Malonyl CoA-acel carrier protein transacylase in human mitochondria associates with respiratory complex one, such that it interacts functionally with a mitochondrial malonyltransferase. Both species are encoded by nuclear genes, and their translocation into mitochondria is dependent on the presence of an N-terminal targeting sequence.[5]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100294 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000048755 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Zhang L, Joshi AK, Smith S (Oct 2003). "Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein". The Journal of Biological Chemistry. 278 (41): 40067–74. doi:10.1074/jbc.M306121200. PMID 12882974.
  6. ^ a b "Entrez Gene: MCAT malonyl CoA:ACP acyltransferase (mitochondrial)".
  7. ^ Kuhl JE, Ruderman NB, Musi N, Goodyear LJ, Patti ME, Crunkhorn S, Dronamraju D, Thorell A, Nygren J, Ljungkvist O, Degerblad M, Stahle A, Brismar TB, Andersen KL, Saha AK, Efendic S, Bavenholm PN (Jun 2006). "Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle". American Journal of Physiology. Endocrinology and Metabolism. 290 (6): E1296-303. doi:10.1152/ajpendo.00341.2005. PMID 16434556.

Further reading edit

  • Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC (Mar 2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
  • Kuhl JE, Ruderman NB, Musi N, Goodyear LJ, Patti ME, Crunkhorn S, Dronamraju D, Thorell A, Nygren J, Ljungkvist O, Degerblad M, Stahle A, Brismar TB, Andersen KL, Saha AK, Efendic S, Bavenholm PN (Jun 2006). "Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle". American Journal of Physiology. Endocrinology and Metabolism. 290 (6): E1296–303. doi:10.1152/ajpendo.00341.2005. PMID 16434556.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I (Jan 2003). "Reevaluating human gene annotation: a second-generation analysis of chromosome 22". Genome Research. 13 (1): 27–36. doi:10.1101/gr.695703. PMC 430954. PMID 12529303.
  • Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.


mcat, gene, malonyl, acyl, carrier, protein, transacylase, mitochondrial, enzyme, that, humans, encoded, mcat, gene, mcatavailable, structurespdbortholog, search, pdbe, rcsblist, codes2c2nidentifiersaliasesmcat, fasn2c, net62, fabd, malonyl, acyl, carrier, pro. Malonyl CoA acyl carrier protein transacylase mitochondrial is an enzyme that in humans is encoded by the MCAT gene 5 6 MCATAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes2C2NIdentifiersAliasesMCAT FASN2C MCT MT NET62 fabD malonyl CoA acyl carrier protein transacylase MCT1External IDsOMIM 614479 MGI 2388651 HomoloGene 15511 GeneCards MCAT OMA MCAT orthologsGene location Human Chr Chromosome 22 human 1 Band22q13 2Start43 132 209 bp 1 End43 143 398 bp 1 Gene location Mouse Chr Chromosome 15 mouse 2 Band15 15 E1Start83 430 998 bp 2 End83 447 988 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inprefrontal cortexkidneybody of stomachsural nerveBrodmann area 9Top expressed inspermatocyteinterventricular septumspermatidseminiferous tubuleproximal tubuleright ventricleleft lobe of liverendocardial cushionbrown adipose tissuesomiteMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functiontransferase activity catalytic activity acyl carrier protein S malonyltransferase activity RNA binding fatty acid synthase activity S malonyltransferase activityCellular componentmitochondrion mitochondrial matrixBiological processmetabolism fatty acid biosynthetic process fatty acid metabolic process lipid metabolism fatty acid beta oxidationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez27349223722EnsemblENSG00000100294ENSMUSG00000048755UniProtQ8IVS2Q8R3F5RefSeq mRNA NM 014507NM 173467NM 001030014RefSeq protein NP 055322NP 775738NP 001025185Location UCSC Chr 22 43 13 43 14 MbChr 15 83 43 83 45 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Clinical significance 3 Interactions 4 References 5 Further readingFunction editThe protein encoded by this gene is found exclusively in the mitochondrion where it catalyzes the transfer of a malonyl group from malonyl CoA to the mitochondrial acyl carrier protein The encoded protein may be part of a fatty acid synthase complex that is more like the type II prokaryotic and plastid complexes rather than the type I human cytosolic complex Two transcript variants encoding different isoforms have been found for this gene 6 Clinical significance editThe enzyme encoded by the MCAT gene along with other enzymes that regulate Malonyl CoA concentration have been shown to regulate levels such that malonyl CoA concentration decreases in human muscle tissue when under exercise training This enzyme specifically has increased activity under these conditions as it is known to catabolize malonyl CoA 7 Interactions editThe human Malonyl CoA acel carrier protein transacylase in human mitochondria associates with respiratory complex one such that it interacts functionally with a mitochondrial malonyltransferase Both species are encoded by nuclear genes and their translocation into mitochondria is dependent on the presence of an N terminal targeting sequence 5 References edit a b c GRCh38 Ensembl release 89 ENSG00000100294 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000048755 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Zhang L Joshi AK Smith S Oct 2003 Cloning expression characterization and interaction of two components of a human mitochondrial fatty acid synthase Malonyltransferase and acyl carrier protein The Journal of Biological Chemistry 278 41 40067 74 doi 10 1074 jbc M306121200 PMID 12882974 a b Entrez Gene MCAT malonyl CoA ACP acyltransferase mitochondrial Kuhl JE Ruderman NB Musi N Goodyear LJ Patti ME Crunkhorn S Dronamraju D Thorell A Nygren J Ljungkvist O Degerblad M Stahle A Brismar TB Andersen KL Saha AK Efendic S Bavenholm PN Jun 2006 Exercise training decreases the concentration of malonyl CoA and increases the expression and activity of malonyl CoA decarboxylase in human muscle American Journal of Physiology Endocrinology and Metabolism 290 6 E1296 303 doi 10 1152 ajpendo 00341 2005 PMID 16434556 Further reading editMa J Dempsey AA Stamatiou D Marshall KW Liew CC Mar 2007 Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects Atherosclerosis 191 1 63 72 doi 10 1016 j atherosclerosis 2006 05 032 PMID 16806233 Kuhl JE Ruderman NB Musi N Goodyear LJ Patti ME Crunkhorn S Dronamraju D Thorell A Nygren J Ljungkvist O Degerblad M Stahle A Brismar TB Andersen KL Saha AK Efendic S Bavenholm PN Jun 2006 Exercise training decreases the concentration of malonyl CoA and increases the expression and activity of malonyl CoA decarboxylase in human muscle American Journal of Physiology Endocrinology and Metabolism 290 6 E1296 303 doi 10 1152 ajpendo 00341 2005 PMID 16434556 Kimura K Wakamatsu A Suzuki Y Ota T Nishikawa T Yamashita R Yamamoto J Sekine M Tsuritani K Wakaguri H Ishii S Sugiyama T Saito K Isono Y Irie R Kushida N Yoneyama T Otsuka R Kanda K Yokoi T Kondo H Wagatsuma M Murakawa K Ishida S Ishibashi T Takahashi Fujii A Tanase T Nagai K Kikuchi H Nakai K Isogai T Sugano S Jan 2006 Diversification of transcriptional modulation large scale identification and characterization of putative alternative promoters of human genes Genome Research 16 1 55 65 doi 10 1101 gr 4039406 PMC 1356129 PMID 16344560 Collins JE Goward ME Cole CG Smink LJ Huckle EJ Knowles S Bye JM Beare DM Dunham I Jan 2003 Reevaluating human gene annotation a second generation analysis of chromosome 22 Genome Research 13 1 27 36 doi 10 1101 gr 695703 PMC 430954 PMID 12529303 Dunham I Shimizu N Roe BA Chissoe S Hunt AR Collins JE Bruskiewich R Beare DM Clamp M Smink LJ Ainscough R Almeida JP Babbage A Bagguley C Bailey J Barlow K Bates KN Beasley O Bird CP Blakey S Bridgeman AM Buck D Burgess J Burrill WD O Brien KP Dec 1999 The DNA sequence of human chromosome 22 Nature 402 6761 489 95 Bibcode 1999Natur 402 489D doi 10 1038 990031 PMID 10591208 nbsp This article on a gene on human chromosome 22 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title MCAT gene amp oldid 1142791541, wikipedia, wiki, book, books, library,

article

, read, download, free, free download, mp3, video, mp4, 3gp, jpg, jpeg, gif, png, picture, music, song, movie, book, game, games.