Carnitine palmitoyltransferase II

Carnitine palmitoyltransferase 2

Identifiers

CPT2 ; CPT1; CPTASE; IIAE4

External IDs

OMIM: 600650 MGI: 109176 HomoloGene: 77 ChEMBL: 3238 GeneCards: CPT2 Gene

2.3.1.21

Gene ontology
Molecular function	• carnitine O-palmitoyltransferase activity
Cellular component	• nucleoplasm • nucleolus • mitochondrion • mitochondrial inner membrane
Biological process	• fatty acid beta-oxidation • carnitine shuttle • cellular lipid metabolic process • small molecule metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
53.2 – 53.21 Mb

Chr 4:
107.9 – 107.92 Mb

PubMed search

Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene.^[1]^[2]

Function

Carnitine palmitoyltransferase II precursor (CPT2) is a nuclear protein which is transported to the mitochondrial inner membrane. CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene are associated with mitochondrial long-chain fatty-acid (LCFA) oxidation disorders and carnitine palmitoyltransferase II deficiency.^[2]

Acyl-CoA from cytosol to the mitochondrial matrix

Model organisms

Model organisms have been used in the study of CPT2 function. A conditional knockout mouse line called Cpt2^{tm1b(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[3] Male and female animals underwent a standardized phenotypic screen^[4] to determine the effects of deletion.^[5]^[6]^[7]^[8] Additional screens performed: - In-depth immunological phenotyping^[9]

*Cpt2* knockout mouse phenotype
Characteristic	Phenotype
All data available at.^[4]^[9]
Peripheral blood leukocytes 6 Weeks	Normal
Haematology 6 Weeks	Normal
Insulin	Normal
Homozygous viability at P14	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Abnormal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Influenza Challenge	Normal

References

↑ Minoletti F, Colombo I, Martin AL, Di Donato S, Taroni F, Finocchiaro G, Pandolfo M (Sep 1992). "Localization of the human gene for carnitine palmitoyltransferase to 1p13-p11 by nonradioactive in situ hybridization". Genomics 13 (4): 1372–1374. doi:10.1016/0888-7543(92)90076-5. PMID 1339389. (Retracted)
1 2 "Entrez Gene: CPT2 carnitine palmitoyltransferase II".
↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
1 2 "International Mouse Phenotyping Consortium".
↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Sanger Institute Mouse Genetics Project, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".

Bonnefont JP, Demaugre F, Prip-Buus C, Saudubray JM, Brivet M, Abadi N, Thuillier L (2000). "Carnitine palmitoyltransferase deficiencies". Mol. Genet. Metab. 68 (4): 424–440. doi:10.1006/mgme.1999.2938. PMID 10607472.
van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes". Mol. Genet. Metab. 71 (1–2): 139–153. doi:10.1006/mgme.2000.3055. PMID 11001805.
Sigauke E, Rakheja D, Kitson K, Bennett MJ (2003). "Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, and molecular review". Lab. Invest. 83 (11): 1543–1554. doi:10.1097/01.LAB.0000098428.51765.83. PMID 14615409.
Taroni F, Verderio E, Fiorucci S, Cavadini P, Finocchiaro G, Uziel G, Lamantea E, Gellera C, DiDonato S (1992). "Molecular characterization of inherited carnitine palmitoyltransferase II deficiency". Proc. Natl. Acad. Sci. U.S.A. 89 (18): 8429–8433. doi:10.1073/pnas.89.18.8429. PMC 49933. PMID 1528846.
Finocchiaro G, Taroni F, Rocchi M, Liras Martin A, Colombo I, Tarelli GT, DiDonato S (1992). "cDNA cloning, sequence analysis, and chromosomal localization of human carnitine palmitoyltransferase". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10981–10981. doi:10.1073/pnas.88.23.10981. PMC 53056. PMID 1961767.
Finocchiaro G, Taroni F, Rocchi M, Martin AL, Colombo I, Tarelli GT, DiDonato S (1991). "cDNA cloning, sequence analysis, and chromosomal localization of the gene for human carnitine palmitoyltransferase". Proc. Natl. Acad. Sci. U.S.A. 88 (2): 661–665. doi:10.1073/pnas.88.2.661. PMC 50872. PMID 1988962.
Finocchiaro G, Colombo I, DiDonato S (1991). "Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver". FEBS Lett. 274 (1–2): 163–166. doi:10.1016/0014-5793(90)81354-Q. PMID 2174799.
Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F (1995). "Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations". Hum. Mol. Genet. 4 (1): 19–29. doi:10.1093/hmg/4.1.19. PMID 7711730.
Britton CH, Schultz RA, Zhang B, Esser V, Foster DW, McGarry JD (1995). "Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 1984–1988. doi:10.1073/pnas.92.6.1984. PMC 42407. PMID 7892212.
Gellera C, Verderio E, Floridia G, Finocchiaro G, Montermini L, Cavadini P, Zuffardi O, Taroni F (1995). "Assignment of the human carnitine palmitoyltransferase II gene (CPT1) to chromosome 1p32". Genomics 24 (1): 195–197. doi:10.1006/geno.1994.1605. PMID 7896283.
Montermini L, Wang H, Verderio E, Taroni F, DiDonato S, Finocchiaro G (1994). "Identification of 5' regulatory regions of the human carnitine palmitoyltransferase II gene". Biochim. Biophys. Acta 1219 (1): 237–40. doi:10.1016/0167-4781(94)90280-1. PMID 8086471.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Taroni F, Verderio E, Dworzak F, Willems PJ, Cavadini P, DiDonato S (1993). "Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients". Nat. Genet. 4 (3): 314–320. doi:10.1038/ng0793-314. PMID 8358442.
Verderio E, Cavadini P, Pandolfo M, DiDonato S, Taroni F (1993). "Two novel sequence polymorphisms of the human carnitine palmitoyltransferase II (CPT1) gene". Hum. Mol. Genet. 2 (3): 334–334. doi:10.1093/hmg/2.3.334. PMID 8499929.
Bonnefont JP, Taroni F, Cavadini P, Cepanec C, Brivet M, Saudubray JM, Leroux JP, Demaugre F (1996). "Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression". Am. J. Hum. Genet. 58 (5): 971–8. PMC 1914604. PMID 8651281.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Wataya K, Akanuma J, Cavadini P, Aoki Y, Kure S, Invernizzi F, Yoshida I, Kira J, Taroni F, Matsubara Y, Narisawa K (1998). "Two CPT2 mutations in three Japanese patients with carnitine palmitoyltransferase II deficiency: functional analysis and association with polymorphic haplotypes and two clinical phenotypes". Hum. Mutat. 11 (5): 377–386. doi:10.1002/(SICI)1098-1004(1998)11:5<377::AID-HUMU5>3.0.CO;2-E. PMID 9600456.
Yang BZ, Ding JH, Dewese T, Roe D, He G, Wilkinson J, Day DW, Demaugre F, Rabier D, Brivet M, Roe C (1998). "Identification of four novel mutations in patients with carnitine palmitoyltransferase II (CPT II) deficiency". Mol. Genet. Metab. 64 (4): 229–236. doi:10.1006/mgme.1998.2711. PMID 9758712.
Taggart RT, Smail D, Apolito C, Vladutiu GD (1999). "Novel mutations associated with carnitine palmitoyltransferase II deficiency". Hum. Mutat. 13 (3): 210–220. doi:10.1002/(SICI)1098-1004(1999)13:3<210::AID-HUMU5>3.0.CO;2-0. PMID 10090476.

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5

2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII

2.3.3: converted into alkyl on transfer	Citrate synthase ATP citrate lyase HMG-CoA synthase Malate synthase

Metabolism: lipid metabolism / fatty acid metabolism, triglyceride and fatty acid enzymes

Synthesis

Malonyl-CoA synthesis	ATP citrate lyase Acetyl-CoA carboxylase

Fatty acid synthesis/ Fatty acid synthase	Beta-ketoacyl-ACP synthase Β-Ketoacyl ACP reductase 3-Hydroxyacyl ACP dehydrase Enoyl ACP reductase

Fatty acid desaturases	Stearoyl-CoA desaturase-1

Triacyl glycerol	Glycerol-3-phosphate dehydrogenase Thiokinase

Degradation

Acyl transport

Beta oxidation

General	Acyl CoA dehydrogenase (ACADL ACADM ACADS ACADVL ACADSB) Enoyl-CoA hydratase MTP: HADH HADHA HADHB Acetyl-CoA C-acyltransferase

Unsaturated	Enoyl CoA isomerase 2,4 Dienoyl-CoA reductase

Odd chain	Propionyl-CoA carboxylase

Other	Hydroxyacyl-Coenzyme A dehydrogenase

To acetyl-CoA

Malonyl-CoA decarboxylase

Aldehydes

Long-chain-aldehyde dehydrogenase

Mitochondrial proteins

Outer membrane

fatty acid degradation	Carnitine palmitoyltransferase I Long-chain-fatty-acid—CoA ligase

tryptophan metabolism	Kynureninase

monoamine neurotransmitter metabolism	Monoamine oxidase

Intermembrane space

Inner membrane

oxidative phosphorylation	Coenzyme Q – cytochrome c reductase Cytochrome c NADH dehydrogenase Succinate dehydrogenase

pyrimidine metabolism	Dihydroorotate dehydrogenase

mitochondrial shuttle	Malate-aspartate shuttle Glycerol phosphate shuttle

other	Glutamate aspartate transporter Glycerol-3-phosphate dehydrogenase ATP synthase Carnitine palmitoyltransferase II Uncoupling protein

Matrix

citric acid cycle	Citrate synthase Aconitase Isocitrate dehydrogenase Oxoglutarate dehydrogenase complex Succinyl coenzyme A synthetase Fumarase Malate dehydrogenase

anaplerotic reactions	Aspartate transaminase Glutamate dehydrogenase Pyruvate dehydrogenase complex

urea cycle	Carbamoyl phosphate synthetase I Ornithine transcarbamylase N-Acetylglutamate synthase

alcohol metabolism	ALDH2

PMPCB

Other/to be sorted

steroidogenesis	Cholesterol side-chain cleavage enzyme Steroid 11-beta-hydroxylase Aldosterone synthase Frataxin

Mitochondrial membrane transport protein Mitochondrial permeability transition pore Mitochondrial carrier

Mitochondrial DNA

Complex I	MT-ND1 MT-ND2 MT-ND3 MT-ND4 MT-ND4L MT-ND5 MT-ND6

Complex III	MT-CYB

Complex IV	MT-CO1 MT-CO2 MT-CO3

ATP synthase	MT-ATP6 MT-ATP8

tRNA	MT-TA MT-TC MT-TD MT-TE MT-TF MT-TG MT-TH MT-TI MT-TK MT-TL1 MT-TL2 MT-TM MT-TN MT-TP MT-TQ MT-TR MT-TS1 MT-TS2 MT-TT MT-TV MT-TW MT-TY

see also mitochondrial diseases

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Carnitine palmitoyltransferase II

Function

Model organisms

See also

References

Further reading