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PROSITE documentation PDOC00402Acyltransferases ChoActase / COT / CPT family signatures
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00402
A number of eukaryotic acetyltransferases can be, on the basis of sequence similarities, grouped together into a family. These enzymes are:
- Choline o-acetyltransferase (EC 2.3.1.6) (ChoAcTase), an enzyme that catalyzes the biosynthesis of the neurotransmitter acetylcholine [1].
- Carnitine o-acetyltransferase (EC 2.3.1.7) [2].
- Peroxisomal carnitine octanoyltransferase (EC 2.3.1.-) (COT), a fatty acid β-oxidation pathway enzyme which is involved in the transport of medium- chain acyl-coenzyme A's from peroxisome to mitochondria [3].
- Mitochondrial carnitine O-palmitoyltransferases I and II (EC 2.3.1.21) (CPT), enzymes involved in fatty acid metabolism and transport [4].
- Yeast hypothetical protein YER024w.
- Mycoplasma pneumoniae putative acetyltransferase C09_orf600.
These enzymes share many regions of sequence similarities. As signature patterns we selected two of these regions. The first one, located in the N-terminal section of these enzymes is characterized by the presence of three [LIVM]-P dipeptides. The second region, located in the central part of these enzymes is characterized by the conservation of a number of charged residues including an histidine which probably plays a crucial role in the catalytic mechanism [5].
Last update:December 2004 / Patterns and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Berrard S. Brice A. Lottspeich F. Braun A. Barde Y.-A. Mallet J. |
| Title | cDNA cloning and complete sequence of porcine choline acetyltransferase: in vitro translation of the corresponding RNA yields an active protein. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 84:9280-9284(1987). | |
| PubMed ID | 3480542 |
| 2 | Authors | Kispal G. Sumegi B. Dietmeier K. Bock I. Gajdos G. Tomcsanyi T. Sandor A. |
| Title | Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae carnitine acetyltransferase. Use of the cDNA in gene disruption studies. | |
| Source | J. Biol. Chem. 268:1824-1829(1993). | |
| PubMed ID | 8420957 |
| 3 | Authors | Chatterjee B. Song C.S. Kim J.-M. Roy A.K. |
| Title | Cloning, sequencing, and regulation of rat liver carnitine octanoyltransferase: transcriptional stimulation of the enzyme during peroxisome proliferation. | |
| Source | Biochemistry 27:9000-9006(1988). | |
| PubMed ID | 3233218 |
| 4 | Authors | Esser V. Britton C.H. Weis B.C. Foster D.W. McGarry J.D. |
| Title | Cloning, sequencing, and expression of a cDNA encoding rat liver carnitine palmitoyltransferase I. Direct evidence that a single polypeptide is involved in inhibitor interaction and catalytic function. | |
| Source | J. Biol. Chem. 268:5817-5822(1993). | |
| PubMed ID | 8449948 |
| 5 | Authors | Schmalix W. Bandlow W. |
| Title | The ethanol-inducible YAT1 gene from yeast encodes a presumptive mitochondrial outer carnitine acetyltransferase. | |
| Source | J. Biol. Chem. 268:27428-27439(1993). | |
| PubMed ID | 8262985 |
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