Identification |
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Name | Carnitine O-acetyltransferase, mitochondrial |
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Synonyms | |
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Gene Name | CAT2 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in acyltransferase activity |
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Specific Function | Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria |
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Cellular Location | Peroxisome. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side |
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SMPDB Pathways | |
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KEGG Pathways | |
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SMPDB Reactions | |
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KEGG Reactions | |
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Metabolites | YMDB ID | Name | View |
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YMDB00045 | Coenzyme A | Show | YMDB00188 | L-Carnitine | Show | YMDB00301 | Palmityl-CoA | Show | YMDB00312 | Acetyl-CoA | Show | YMDB00351 | L-Acetylcarnitine | Show | YMDB00438 | S-Adenosyl-L-methionine | Show | YMDB00616 | (R)-Carnitine | Show | YMDB00617 | O-acetylcarnitinium | Show | YMDB01534 | Hexadecanoylcarnitine | Show |
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GO Classification | Component |
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Not Available | Function |
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catalytic activity | transferase activity | transferase activity, transferring acyl groups | transferase activity, transferring acyl groups other than amino-acyl groups | acyltransferase activity | Process |
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Not Available |
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Gene Properties |
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Chromosome Location | chromosome 13 |
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Locus | YML042W |
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Gene Sequence | >2013 bp
ATGAGGATCTGTCATTCGAGAACTCTCTCAAACTTAAAGGATCTTCCGATAACGTCAAGG
AGAGCAATGCATTCGGCCATTGTCAATTACTCCACCCAAAAGGCCCAATTTCCCGTAGAG
ACAAATAATGGGGAACACTATTGGGCGGAAAAGCCGAACAAATTCTACCAGAACAAAAGG
CCCAATTTTCAAGGCATTACCTTTGCTAAACAACAAGACTTACCATCATTACCCGTGCCC
GAATTGAAGTCTACACTTGACAAGTATTTGCAAACCATCCGCCCATTTTGCAATGATGTA
GAAACTTTTGAAAGACAGCAGCTGTTATGTAAGGACTTCTCGGAGCACATGGGGCCTATC
TTACAAGACCGATTGAAAGAGTATGCCAACGATAAAAGAAACTGGATGGCCAAGTTTTGG
GATGAACAATCCTATTTACAATACAACGATCCTATTGTTCCATACGTCTCTTATTTTTAT
TCTCATATGCCATTACCGAATCATTTATCGAAGATCGATAATGATCCTTTGATTAAGGCT
ACTGCGATTATCTCAACCGTGGTTAAATTCATCGAAGCTATTAAAGATGAATCTTTACCC
GTAGAAATTATCAAAGGTATGCCATTTTGTATGAATAGTTTTTCATTGATGTTTAACACT
TCGAGATTGCCTGGTAAGCCAGAGGATAACCAAGATACAAATATTTTTTATTCAGTTTAT
GAGAACAACTTTGTAACTATCGCTTATAAAGGGAAGTTTTACAAACTGATGACCCATGAC
GGGAATCACAAACCGCTTTCCGAAAACGAAATCTGGAGGCAACTGTACTCTGTGGTATTC
CAAGGATCGCAGTCCGATCCCAAACTAGGTGGCATTGGTTCTCTCACCTCTTTACCTCGT
GATCAATGGCGTGAAGTACATATGGAGCTTATGAAGGATCCTATTTCTCAGGATTCACTA
GAAACAATCCATAAGTCTTCCTTTATGCTATGTTTGGATCTTGACCAATCCCCTGTCACT
TTGGAAGAAAAGTCAAGAAATTGCTGGCACGGTGATGGTATTAACAGATTCTACGATAAG
TCTTTACAGTTCCTAGTCACCGGTAATGGTTCATCAGGTTTCTTAGCTGAACACTCGAAG
ATGGATGGTACGCCAACATTGTTTTTAAATAACTACGTTTGTCAGCAGTTGAATAAACTA
GATGTGGATGACTTCATGAGAAAAGTAATTACGCCATCATCTACGGTGGCAATGAAACCT
ATGGAACTGCCCTTCATTATCACACCGAAGATTCATAAAGCAATCGAATCTGCCCAACTA
CAATTTAAGGAAACAATTGGTGAGCATGACCTACGTGTTTGGCACTACAACAAATATGGA
AAAACGTTTATAAAACGCCATGGCATGTCACCTGATGCATTTATTCAACAAGTTATCCAA
CTGGCGGTTTTCAAATATCTGAAACGACAACTACCAACTTACGAGGCTGCTTCCACGAGA
AAATACTTCAAAGGCCGTACTGAAACTGGTAGATCTGTGTCCACCGCCTCCTTAGAATTT
GTTTCTAAATGGCAAAATGGCGATGTTCCTATTGCAGAAAAGATTCAGGCTTTGAAACAT
TCTGCAAAAGAGCATTCGACGTACCTGAAAAATGCTGCAAATGGTAATGGTGTCGATCGT
CATTTCTTCGGTCTAAAGAATATGCTAAAATCTAATGATGACCAAATTCCGCCCCTTTTC
AAAGATCCCTTATTTAATTATTCTTCAACTTGGTTGATCTCCACATCTCAACTATCTTCG
GAATATTTTGACGGTTATGGTTGGTCCCAAGTAAATGACAACGGGTTTGGACTGGCATAC
ATGTTGAATAACGAGTGGCTGCATATCAATATTGTCAACAAACCAGCCAAGAGTGGAGCC
AGTGTTAACAGATTACACTATTATTTATCTCAAGCTGCTGATGAAATTTTTGACGCCTTG
GAAAATGAGAATAAACGAAAAGCAAAGTTATGA |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 670 |
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Protein Molecular Weight | 77241.20313 |
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Protein Theoretical pI | 8.4 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Carnitine O-acetyltransferase, mitochondrial
MRICHSRTLSNLKDLPITSRRAMHSAIVNYSTQKAQFPVETNNGEHYWAEKPNKFYQNKR
PNFQGITFAKQQDLPSLPVPELKSTLDKYLQTIRPFCNDVETFERQQLLCKDFSEHMGPI
LQDRLKEYANDKRNWMAKFWDEQSYLQYNDPIVPYVSYFYSHMPLPNHLSKIDNDPLIKA
TAIISTVVKFIEAIKDESLPVEIIKGMPFCMNSFSLMFNTSRLPGKPEDNQDTNIFYSVY
ENNFVTIAYKGKFYKLMTHDGNDKPLSENEIWRQLYSVVFQGSQSDPKLGGIGSLTSLPR
DQWREVHLELMKDPISQDSLETIHKSSFMLCLDLDQSPVTLEEKSRNCWHGDGINRFYDK
SLQFLVTGNGSSGFLAEHSKMDGTPTLFLNNYVCQQLNKLDVDDFMRKVITPSSTVAMKP
MELPFIITPKIHKAIESAQLQFKETIGEHDLRVWHYNKYGKTFIKRHGMSPDAFIQQVIQ
LAVFKYLKRQLPTYEAASTRKYFKGRTETGRSVSTASLEFVSKWQNGDVPIAEKIQALKH
SAKEHSTYLKNAANGNGVDRHFFGLKNMLKSNDDQIPPLFKDPLFNYSSTWLISTSQLSS
EYFDGYGWSQVNDNGFGLAYMLNNEWLHINIVNKPAKSGASVNRLHYYLSQAADEIFDAL
ENENKRKAKL |
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References |
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External Links | |
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General Reference | - Kispal, G., Sumegi, B., Dietmeier, K., Bock, I., Gajdos, G., Tomcsanyi, T., Sandor, A. (1993). "Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae carnitine acetyltransferase. Use of the cDNA in gene disruption studies." J Biol Chem 268:1824-1829.8420957
- Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
- Elgersma, Y., van Roermund, C. W., Wanders, R. J., Tabak, H. F. (1995). "Peroxisomal and mitochondrial carnitine acetyltransferases of Saccharomyces cerevisiae are encoded by a single gene." EMBO J 14:3472-3479.7628448
- Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
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