MCAT (gene)

MCAT
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2C2N
Identifiers
Aliases	MCAT , FASN2C, MCT, MT, NET62, fabD, malonyl-CoA-acyl carrier protein transacylase, MCT1
External IDs	OMIM: 614479 MGI: 2388651 HomoloGene: 15511 GeneCards: MCAT
Gene location (Human)
Chr.	Chromosome 22 (human)
End	43,143,398 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	83,447,988 bp
RNA expression pattern
	Top expressed in
	prefrontal cortex; ; kidney; ; body of stomach; ; sural nerve; ; Brodmann area 9;
	Top expressed in
	spermatocyte; ; interventricular septum; ; spermatid; ; seminiferous tubule; ; proximal tubule; ; right ventricle; ; left lobe of liver; ; endocardial cushion; ; brown adipose tissue; ; somite;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity ; catalytic activity ; [acyl-carrier-protein S-malonyltransferase activity]; RNA binding ; fatty acid synthase activity ; S-malonyltransferase activity ;
Cellular component	mitochondrion ; mitochondrial matrix ;
Biological process	metabolism ; fatty acid biosynthetic process ; fatty acid metabolic process ; lipid metabolism ; fatty acid beta-oxidation ;
	Sources:Amigo / QuickGO
Orthologs
	27349
	223722
	ENSG00000100294
	ENSMUSG00000048755
	Q8IVS2
	Q8R3F5
	NM_014507 ; NM_173467
	NM_001030014
	NP_055322 ; NP_775738
	NP_001025185
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 05, 2023

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

Function

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

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

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]

Related Research Articles

<span class="mw-page-title-main">Malonyl-CoA</span> Chemical compound

Malonyl-CoA is a coenzyme A derivative of malonic acid.

<span class="mw-page-title-main">Chromosome 22</span> Human chromosome

Chromosome 22 is one of the 23 pairs of chromosomes in human cells. Humans normally have two copies of chromosome 22 in each cell. Chromosome 22 is the second smallest human chromosome, spanning about 51 million DNA base pairs and representing between 1.5 and 2% of the total DNA in cells.

Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. This gene encodes a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. This enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. The ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency.

<span class="mw-page-title-main">Malonyl-CoA decarboxylase</span> Class of enzymes

Malonyl-CoA decarboxylase, is found in bacteria and humans and has important roles in regulating fatty acid metabolism and food intake, and it is an attractive target for drug discovery. It is an enzyme associated with Malonyl-CoA decarboxylase deficiency. In humans, it is encoded by the MLYCD gene.

Carnitine palmitoyltransferase I (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase (CCAT), or palmitoylCoA transferase I, is a mitochondrial enzyme responsible for the formation of acyl carnitines by catalyzing the transfer of the acyl group of a long-chain fatty acyl-CoA from coenzyme A to l-carnitine. The product is often Palmitoylcarnitine, but other fatty acids may also be substrates. It is part of a family of enzymes called carnitine acyltransferases. This "preparation" allows for subsequent movement of the acyl carnitine from the cytosol into the intermembrane space of mitochondria.

Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT1 gene.

In enzymology, a [acyl-carrier-protein] S-acetyltransferase is an enzyme that catalyzes the reversible chemical reaction

In enzymology, a [acyl-carrier-protein] S-malonyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II (EC 2.3.1.179) is an enzyme that catalyzes the chemical reaction

Peroxisomal membrane protein PMP34 is a protein that in humans is encoded by the SLC25A17 gene.

Acyl-CoA thioesterase 2, also known as ACOT2, is an enzyme which in humans is encoded by the ACOT2 gene.

Acyl-coenzyme A thioesterase 4 is an enzyme that in humans is encoded by the ACOT4 gene.

Acyl-coenzyme A thioesterase 11 also known as StAR-related lipid transfer protein 14 (STARD14) is an enzyme that in humans is encoded by the ACOT11 gene. This gene encodes a protein with acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates which relies on its StAR-related lipid transfer domain. Expression of a similar murine protein in brown adipose tissue is induced by cold exposure and repressed by warmth. Expression of the mouse protein has been associated with obesity, with higher expression found in obesity-resistant mice compared with obesity-prone mice. Alternative splicing results in two transcript variants encoding different isoforms.

MCAT is the Medical College Admission Test.

Acyl-CoA thioesterase 6 is a protein that in humans is encoded by the ACOT6 gene. The protein, also known as C14orf42, is an enzyme with thioesterase activity.

Acyl-CoA synthetase family member 3 is an enzyme that in humans is encoded by the ACSF3 gene.

Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase superfamily, which is a group of enzymes that hydrolyze Coenzyme A esters. There is no known function, however it has been shown to act as a long-chain thioesterase at low concentrations, and a short-chain thioesterase at high concentrations.

Acyl-CoA thioesterase 13 is a protein that in humans is encoded by the ACOT13 gene. This gene encodes a member of the thioesterase superfamily. In humans, the protein co-localizes with microtubules and is essential for sustained cell proliferation.

Acyl-CoA thioesterase 1 is a protein that in humans is encoded by the ACOT1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100294 - Ensembl, May 2017
1 2 3 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.
1 2 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.
1 2 "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.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100294 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid12882974-5] 1 2 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.

[entrez-6] 1 2 "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.

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