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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/01 13:29:32」(JST)

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Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3.1.21) involved in the metabolism of palmitoylcarnitine into palmitoyl-CoA. A related transferase is carnitine acyltransferase.

Molecules[edit]

Palmitoylcarnitine
Palmitoyl CoA

Pathway[edit]

Acyl-CoA from cytosol to the mitochondrial matrix

Human forms of CPT[edit]

There are four different forms of CPT in humans:

CPT1A - associated with Carnitine palmitoyltransferase I deficiency
CPT1B
CPT1C
CPT2 - associated with Carnitine palmitoyltransferase II deficiency

References[edit]

^ Jogl G, Tong L (January 2003). "Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport". Cell 112 (1): 113–22. doi:10.1016/S0092-8674(02)01228-X. PMID 12526798.

External links[edit]

PDOC00402 - Acyltransferases ChoActase / COT / CPT family in PROSITE
Choline/Carnitine o-acyltransferase family in Pfam
UMich Orientation of Proteins in Membranes protein/pdbid-2h4t
Carnitine O-Palmitoyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1.

Samanta S1, Situ AJ, Ulmer TS.Author information 1Department of Biochemistry & Molecular Biology and Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90033.AbstractNeurons contain a mammalian-specific isoform of the enzyme carnitine palmitoyltransferase 1 (CPT1C) that couples malonyl-CoA to ceramide levels thereby contributing to systemic energy homeostasis and feeding behavior. In contrast to CPT1A, which controls the rate-limiting step of long-chain fatty acid β-oxidation in all tissues, the biochemical context and regulatory mechanism of CPT1C are unknown. CPT1 enzymes are comprised of an N-terminal regulatory domain and a C-terminal catalytic domain (CD) that are separated by two transmembrane helices. In CPT1A, the regulatory domain, termed N, adopts an inhibitory and non-inhibitory state, Nα and Nβ, respectively, which differ in their association with the CD. To provide insight into the regulatory mechanism of CPT1C, we have determined the structure of its regulatory domain (residues Met1-Phe50) by NMR spectroscopy. In relation to CPT1A, the inhibitory Nα state was found to be structurally homologues whereas the non-inhibitory Nβ state was severely destabilized, suggesting a change in overall regulation. The destabilization of Nβ may contribute to the low catalytic activity of CPT1C relative to CPT1A and makes its association with the CD unlikely. In analogy to the stabilization of Nβ by the CPT1A CD, non-inhibitory interactions of N of CPT1C with another protein may exist. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 398-405, 2014.
Biopolymers.Biopolymers.2014 Apr;101(4):398-405. doi: 10.1002/bip.22396.
Neurons contain a mammalian-specific isoform of the enzyme carnitine palmitoyltransferase 1 (CPT1C) that couples malonyl-CoA to ceramide levels thereby contributing to systemic energy homeostasis and feeding behavior. In contrast to CPT1A, which controls the rate-limiting step of long-chain fatty ac
PMID 24037959

Carnitine palmitoyltransferase II (CPT II) deficiency: Genotype-Phenotype analysis of 50 patients.

Joshi PR1, Deschauer M2, Zierz S2.Author information 1Department of Neurology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany. Electronic address: pushpa.joshi@medizin.uni-halle.de.2Department of Neurology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.AbstractClinical, biochemical and molecular genetic data in a cohort of 50 patients with muscle CPT II deficiency are reported. Attacks of myoglobinuria occurred in 86% of patients. In 94% of patients the triggering factor was exercise. Although the myopathic form is often called the adult from, in 60% of patients, the age of onset was in childhood (1-12years). All the patients in whom biochemical activity was measured had normal enzyme activity of total CPT I+II but the activity was significantly inhibited by malonyl-CoA and Triton. The p.S113L mutation was detected in 38/40 index patients (95%) in at least one allele. Sixty percent of index patients were homozygous for this mutation. Thirteen other mutations, all in compound heterozygote form, were also identified. There was no significant difference in ages of onset, clinical and biochemical phenotype of patients with p.S113L mutation in homozygous or compound heterozygous form. The exception was a tendency of slightly higher residual enzyme activity upon malonyl-CoA inhibition in compound heterozygotes. Phenotype was also not significantly different in patients with missense mutations on both alleles and patients with truncating mutation on one allele and missense mutation on the other allele. However, the only exception was that, attacks were triggered by fasting in almost all the patients with truncating mutations. In contrast, fasting triggered the attacks only in one third of patients with missense mutations on both alleles. The data indicate that within the muscle form of CPT II deficiency, the various genotypes have only marginal influence on the clinical and biochemical phenotype.
Journal of the neurological sciences.J Neurol Sci.2014 Mar 15;338(1-2):107-11. doi: 10.1016/j.jns.2013.12.026. Epub 2013 Dec 23.
Clinical, biochemical and molecular genetic data in a cohort of 50 patients with muscle CPT II deficiency are reported. Attacks of myoglobinuria occurred in 86% of patients. In 94% of patients the triggering factor was exercise. Although the myopathic form is often called the adult from, in 60% of p
PMID 24398345

AMPK in the Small Intestine in Normal and Pathophysiological Conditions.

Harmel E1, Grenier E, Bendjoudi Ouadda A, El Chebly M, Ziv E, Beaulieu JF, Sané A, Spahis S, Laville M, Levy E.Author information 1Research Center (E.H., E.G., A.B.O., M.E.C., A.S., S.S., E.L.), Sainte-Justine MUHC, Montreal, Quebec, Canada, H3T 1C5; Department of Nutrition (E.H., E.G., S.S., E.L.) and Department of Biochemistry (M.E.C.), Université de Montréal, Montreal, Quebec, Canada, H3T 1C5; Diabetes Unit (E.Z.), Division of Internal Medicine, Hadassah Ein Kerem Hospital, 120 Jerusalem, Israel-91; Canadian Institutes for Health Research Team on the Digestive Epithelium (J.F.B., E.L.), Department of Anatomy and Cellular Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec, Canada, J1H 5N4; and CRNH Rhône-Alpes (E.H., M.L.), Université Lyon 1, Institut National de la Santé et de la Recherche Médicale Unité Mixte de Recherche 1060, CENS, Centre Hospitalier Lyon-Sud, F-69310 Pierre Bénite, France.AbstractThe role of AMPK in regulating energy storage and depletion remains unexplored in the intestine. This study will to define its status, composition, regulation and lipid function, as well as to examine the impact of insulin resistance and type 2 diabetes on intestinal AMPK activation, insulin sensitivity, and lipid metabolism. Caco-2/15 cells and Psammomys obesus (P. obesus) animal models were experimented. We showed the predominance of AMPKα1 and the prevalence of α1/β2/γ1 heterotrimer in Caco-2/15 cells. The activation of AMPK by 5-aminoimidazole-4-carboxamide ribonucleoside and metformin resulted in increased phospho(p)-ACC. However, the down-regulation of p-AMPK by compound C and high glucose lowered p-ACC without affecting 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Administration of metformin to P. obesus with insulin resistance and type 2 diabetes led to 1) an up-regulation of intestinal AMPK signaling pathway typified by ascending p-AMPKα(-Thr172); 2) a reduction in ACC activity; 3) an elevation of carnitine palmitoyltransferase 1; 4) a trend of increase in insulin sensitivity portrayed by augmentation of p-Akt and phospho-glycogen synthetase kinase 3β; 5) a reduced phosphorylation of p38-MAPK and ERK1/2; and 6) a decrease in diabetic dyslipidemia following lowering of intracellular events that govern lipoprotein assembly. These data suggest that AMPK fulfills key functions in metabolic processes in the small intestine.
Endocrinology.Endocrinology.2014 Mar;155(3):873-88. doi: 10.1210/en.2013-1750. Epub 2014 Jan 1.
The role of AMPK in regulating energy storage and depletion remains unexplored in the intestine. This study will to define its status, composition, regulation and lipid function, as well as to examine the impact of insulin resistance and type 2 diabetes on intestinal AMPK activation, insulin sensiti
PMID 24424053

Japanese Journal

Carnitine palmitoyltransferase 2 gene polymorphism is a genetic risk factor for sudden unexpected death in infancy

Yamamoto Takuma,Tanaka Hidekazu,Emoto Yuko,Umehara Takahiro,Fukahori Yuki,Kuriu Yukiko,Matoba Ryoji,Ikematsu Kazuya
Brain and Development 36(6), 479-483, 2014-05
… Rationale: Carnitine palmitoyltransferase (CPT) II is one of a pivotal enzyme in mitochondrial fatty acid oxidation, which is essential for energy production during simultaneous glucose sparing and a requirement for major energy supply, such as prolonged fasting or exercise. …
NAID 120005477103

Mechanisms of exercise- and training-induced fatty acid oxidation in skeletal muscle

Miura Shinji,Tadaishi Miki,Kamei Yasutomi [他],Ezaki Osamu
The Journal of Physical Fitness and Sports Medicine 3(1), 43-53, 2014
… Carnitine palmitoyltransferase 1 (CPT1), which regulates the β-oxidation of fatty acids in mitochondria, is believed to play an important role in the acute effect. …
NAID 130003397904

カルニチンパルミトイルトランスフェラーゼ-I欠損症のスクリーニング指標の妥当性の検討

重松陽介,畑郁江,伊藤順庸,新井田要,但馬剛,田崎隆二,新宅治夫,小林弘典,大浦敏博
日本マス・スクリーニング学会誌 = Journal of Japanese Society for Mass-screening 23(1), 93-97, 2013-06-01
NAID 10031183097

「カルニチンパルミトイルトランスフェラーゼ」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Choline/Carnitine o-acyltransferase
	; Structure of carnitine acetyltransferase.
Identifiers
Symbol	Carn_acyltransf
Pfam	PF00755
Pfam clan	CL0149
InterPro	IPR000542
PROSITE	PDOC00402
SCOP	1ndi
SUPERFAMILY	1ndi
OPM superfamily	183
OPM protein	2h3u
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary