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Choline acetyltransferase
Identifiers
EC number 2.3.1.6
CAS number 9012-78-6
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Gene Ontology AmiGO / EGO
edit
Choline acetyltransferase

PDB rendering based on 2fy2.
Available structures
2fy2, 2fy3, 2fy4, 2fy5
Identifiers
Symbols CHAT; CMS1A; CMS1A2
External IDs OMIM: 118490 MGI: 88392 HomoloGene: 40693 GeneCards: CHAT Gene
EC number 2.3.1.6
RNA expression pattern
PBB GE CHAT 221197 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1103 12647
Ensembl ENSG00000070748 ENSMUSG00000021919
UniProt P28329 Q8BQN4
RefSeq (mRNA) NM_020549 NM_009891
RefSeq (protein) NP_065574 NP_034021
Location (UCSC) Chr 10:
50.49 - 50.54 Mb		 Chr 14:
31.24 - 31.29 Mb
PubMed search [1] [2]

Choline acetyltransferase (abbreviated "ChAT") is an enzyme that is synthesized within the body of a neuron. It is then transferred to the nerve terminal via axoplasmic flow. The role of choline acetyltransferase is to join Acetyl-CoA to choline, resulting in the formation of the neurotransmitter acetylcholine.[1] In humans, the choline acetyltransferase enyzme is encoded by the CHAT gene.[2]

Contents

Function

Cholinergic systems are implicated in numerous neurologic functions. Alteration in some cholinergic neurons may account for the disturbances of Alzheimer disease. The protein encoded by this gene synthesizes the neurotransmitter acetylcholine. Alternative splice variants have been found that contain alternative 5' untranslated exons. Three of the four described splice variants encode identical 69 kDa proteins while one variant encodes both the 69 kDa and a larger 82 kDa protein.[1]

Choline

Acetylcholine

It is often used as a marker, immunohistochemically, for motor neurons (motoneurons).

See also

References

  1. ^ a b "Entrez Gene: CHAT choline acetyltransferase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1103.  
  2. ^ Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (February 1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–8. PMID 1840566.  

Further reading

  • Oda Y (2000). "Choline acetyltransferase: the structure, distribution and pathologic changes in the central nervous system". Pathol. Int. 49 (11): 921–37. doi:10.1046/j.1440-1827.1999.00977.x. PMID 10594838.  
  • Oda Y, Nakanishi I, Deguchi T (1993). "A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells". Brain Res. Mol. Brain Res. 16 (3-4): 287–94. doi:10.1016/0169-328X(92)90237-6. PMID 1337937.  
  • Toussaint JL, Geoffroy V, Schmitt M, et al. (1992). "Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions". Genomics 12 (2): 412–6. doi:10.1016/0888-7543(92)90395-9. PMID 1339386.  
  • Lorenzi MV, Trinidad AC, Zhang R, Strauss WL (1992). "Two mRNAs are transcribed from the human gene for choline acetyltransferase". DNA Cell Biol. 11 (8): 593–603. doi:10.1089/dna.1992.11.593. PMID 1388731.  
  • Misawa H, Ishii K, Deguchi T (1992). "Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region". J. Biol. Chem. 267 (28): 20392–9. PMID 1400357.  
  • Cervini R, Rocchi M, DiDonato S, Finocchiaro G (1992). "Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene". Neurosci. Lett. 132 (2): 191–4. doi:10.1016/0304-3940(91)90299-9. PMID 1784419.  
  • Strauss WL, Kemper RR, Jayakar P, et al. (1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–8. doi:10.1016/0888-7543(91)90273-H. PMID 1840566.  
  • Viegas-Péquignot E, Berrard S, Brice A, et al. (1991). "Localization of a 900-bp-long fragment of the human choline acetyltransferase gene to 10q11.2 by nonradioactive in situ hybridization". Genomics 9 (1): 210–2. doi:10.1016/0888-7543(91)90242-7. PMID 2004764.  
  • Itoh N, Slemmon JR, Hawke DH, et al. (1986). "Cloning of Drosophila choline acetyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (11): 4081–5. doi:10.1073/pnas.83.11.4081. PMID 3086876.  
  • Hersh LB, Takane K, Gylys K, et al. (1988). "Conservation of amino acid sequences between human and porcine choline acetyltransferase". J. Neurochem. 51 (6): 1843–5. doi:10.1111/j.1471-4159.1988.tb01166.x. PMID 3183663.  
  • Berrard S, Brice A, Lottspeich F, et al. (1988). "cDNA cloning and complete sequence of porcine choline acetyltransferase: in vitro translation of the corresponding RNA yields an active protein". Proc. Natl. Acad. Sci. U.S.A. 84 (24): 9280–4. doi:10.1073/pnas.84.24.9280. PMID 3480542.  
  • Chireux MA, Le Van Thai A, Weber MJ (1995). "Human choline acetyltransferase gene: localization of alternative first exons". J. Neurosci. Res. 40 (4): 427–38. doi:10.1002/jnr.490400402. PMID 7616604.  
  • Bausero P, Schmitt M, Toussaint JL, et al. (1993). "Identification and analysis of the human choline acetyltransferase gene promoter". Neuroreport 4 (3): 287–90. doi:10.1097/00001756-199303000-00015. PMID 7682855.  
  • Quirin-Stricker C, Nappey V, Simoni P, et al. (1994). "Trans-activation by thyroid hormone receptors of the 5' flanking region of the human ChAT gene". Brain Res. Mol. Brain Res. 23 (3): 253–65. doi:10.1016/0169-328X(94)90232-1. PMID 8057782.  
  • Erickson JD, Varoqui H, Schäfer MK, et al. (1994). "Functional identification of a vesicular acetylcholine transporter and its expression from a "cholinergic" gene locus". J. Biol. Chem. 269 (35): 21929–32. PMID 8071310.  
  • Kengaku M, Misawa H, Deguchi T (1993). "Multiple mRNA species of choline acetyltransferase from rat spinal cord". Brain Res. Mol. Brain Res. 18 (1-2): 71–6. doi:10.1016/0169-328X(93)90174-N. PMID 8479291.  
  • Misawa H, Matsuura J, Oda Y, et al. (1997). "Human choline acetyltransferase mRNAs with different 5'-region produce a 69-kDa major translation product". Brain Res. Mol. Brain Res. 44 (2): 323–33. doi:10.1016/S0169-328X(96)00231-8. PMID 9073174.  
  • Lönnerberg P, Ibáñez CF (1999). "Novel, testis-specific mRNA transcripts encoding N-terminally truncated choline acetyltransferase". Mol. Reprod. Dev. 53 (3): 274–81. doi:10.1002/(SICI)1098-2795(199907)53:3<274::AID-MRD3>3.0.CO;2-8. PMID 10369388.  
  • Sakakibara A, Hattori S (2000). "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways". J. Biol. Chem. 275 (9): 6404–10. doi:10.1074/jbc.275.9.6404. PMID 10692442.  

External links

Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups
(mostly acetyltransferases)
2.3.2: Aminoacyltransferases
2.3.3: converted into alkyl on transfer
Metabolism: amino acid metabolism - neurotransmitter enzymes
monoamine
arginine→NO
choline→Acetylcholine
anabolism: Choline acetyltransferase
catabolism: Cholinesterase (Acetylcholinesterase, Butyrylcholinesterase)
see also intermediates







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