| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-07-31 17:02:22 |
| Accession Number |
HMDB00895 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Acetylcholine |
| Description |
Acetylcholine (ACh) is a neurotransmitter. Acetylcholine in vertebrates is the major transmitter at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system. Its physiological and pharmacological effects, metabolism, release, and receptors have been well documented in several species. ACh has been considered an important excitatory neurotransmitter in the carotid body (CB). Various nicotinic and muscarinic ACh receptors are present in both afferent nerve endings and glomus cells. Therefore, ACh can depolarize or hyperpolarize the cell membrane depending on the available receptor type in the vicinity. Binding of ACh to its receptor can create a wide variety of cellular responses including opening cation channels (nicotinic ACh receptor activation), releasing Ca2+ from intracellular storage sites (via muscarinic ACh receptors), and modulating activities of K+ and Ca2+ channels. Interactions between ACh and other neurotransmitters (dopamine, adenosine, nitric oxide) have been known, and they may induce complicated responses. Cholinergic biology in the CB differs among species and even within the same species due to different genetic composition. Development and environment influence cholinergic biology.
Pharmacological data clearly indicate that both muscarinic and nicotinic acetylcholine receptors have a role in the encoding of new memories. Localized lesions and antagonist infusions demonstrate the anatomical locus of these cholinergic effects, and computational modeling links the function of cholinergic modulation to specific cellular effects within these regions. Acetylcholine has been shown to increase the strength of afferent input relative to feedback, to contribute to theta rhythm oscillations, activate intrinsic mechanisms for persistent spiking, and increase the modification of synapses. These effects might enhance different types of encoding in different cortical structures. In particular, the effects in entorhinal and perirhinal cortex and hippocampus might be important for encoding new episodic memories.
The role of ACh in attention has been repeatedly demonstrated in several tasks. Acetylcholine is linked to response accuracy in voluntary and reflexive attention and also to response speed in reflexive attention. It is well known that those with Attention-deficit/hyperactivity disorders tend to be inaccurate and slow to respond. (PMID: 17284361, 17011181, 15556286) |
| Synonyms |
- ACh
- Acetyl choline ion
- Acetylcholine cation
- Acetylcholinium: acetyl-Choline
- Choline acetate
- Choline acetate (ester)
- O-acetylcholine
|
| Chemical IUPAC Name |
2-acetyloxyethyl-trimethyl-ammonium |
| Chemical Formula |
C7H16NO2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
- Short chain acyl carnitines
|
| Family |
|
| Species |
- cation
- quaternary ammonium salt
- carboxylic acid ester
|
| Biofunction |
- Component of Glycerophospholipid metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
146.207 |
| Monoisotopic Molecular Weight |
146.118103 |
| Isomeric SMILES |
CC(=O)OCC[N+](C)(C)C |
| Canonical SMILES |
CC(=O)OCC[N+](C)(C)C |
| KEGG Compound ID |
C01996  |
| BioCyc ID |
ACETYLCHOLINE  |
| BiGG ID |
38868  |
| Wikipedia Link |
Acetylcholine  |
| NuGOwiki Link |
HMDB00895  |
| Metagene Link |
HMDB00895  |
| METLIN ID |
57  |
| PubChem Compound |
187  |
| PubChem Substance |
148633  |
| ChEBI ID |
15355  |
| CAS Registry Number |
51-84-3 |
| InChI Identifier |
InChI=1/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 |
| Synthesis Reference |
Szutowicz, Andrzej. Acetylcholine synthesis in synaptosomes. Postepy Biochemii (1979), 25(1), 59-84. |
| Melting Point (Experimental) |
148 oC |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 0.136 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.91 [Predicted by ALOGPS]; -3.45 [MEYLAN,WM & HOWARD,PH (1995)]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
2ACE  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Show Image Show Peaklist |
| BMRB Spectrum |
Show Image Show Peaklist |
| Cellular Location |
- Cytoplasm
- Extracellular
- nucleus
|
| Biofluid Location |
- Cerebrospinal Fluid
- Urine
|
| Tissue Location |
| Tissue |
References |
| Adipose Tissue |
— |
| Adrenal Medulla |
— |
| Bladder |
— |
| Brain |
— |
| Fibroblasts |
— |
| Intestine |
— |
| Kidney |
— |
| Lung |
— |
| Muscle |
— |
| Myelin |
— |
| Nerve Cells |
— |
| Neuron |
— |
| Pancreas |
— |
| Placenta |
— |
| Platelet |
— |
| Prostate |
— |
| Skeletal Muscle |
— |
| Skin |
— |
| Spleen |
— |
| Testes |
— |
|
| Concentrations (Normal) |
| Biofluid |
CSF |
| Value |
0.034 +/- 0.009 uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Jia JP, Jia JM, Zhou WD, Xu M, Chu CB, Yan X, Sun YX: Differential acetylcholine and choline concentrations in the cerebrospinal fluid of patients with Alzheimer's disease and vascular dementia. Chin Med J (Engl). 2004 Aug;117(8):1161-4. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.078 +/- 0.074 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Adults |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
|
| Concentrations (Abnormal) |
| Biofluid |
CSF |
| Value |
0.01 +/- 0.005 uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Jia JP, Jia JM, Zhou WD, Xu M, Chu CB, Yan X, Sun YX: Differential acetylcholine and choline concentrations in the cerebrospinal fluid of patients with Alzheimer's disease and vascular dementia. Chin Med J (Engl). 2004 Aug;117(8):1161-4. [PubMed
]
|
| Biofluid |
CSF |
| Value |
0.016 +/- 0.007 uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Condition |
Multi-infarct dementia |
| Comments |
Not Available |
| References |
- Jia JP, Jia JM, Zhou WD, Xu M, Chu CB, Yan X, Sun YX: Differential acetylcholine and choline concentrations in the cerebrospinal fluid of patients with Alzheimer's disease and vascular dementia. Chin Med J (Engl). 2004 Aug;117(8):1161-4. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Alzheimer's disease |
- Jia JP, Jia JM, Zhou WD, Xu M, Chu CB, Yan X, Sun YX: Differential acetylcholine and choline concentrations in the cerebrospinal fluid of patients with Alzheimer's disease and vascular dementia. Chin Med J (Engl). 2004 Aug;117(8):1161-4. [PubMed
]
|
| Multi-infarct dementia |
- Jia JP, Jia JM, Zhou WD, Xu M, Chu CB, Yan X, Sun YX: Differential acetylcholine and choline concentrations in the cerebrospinal fluid of patients with Alzheimer's disease and vascular dementia. Chin Med J (Engl). 2004 Aug;117(8):1161-4. [PubMed
]
|
|
| OMIM ID |
|
| Pathways |
|
| General References |
- Nguyen VT, Ndoye A, Hall LL, Zia S, Arredondo J, Chernyavsky AI, Kist DA, Zelickson BD, Lawry MA, Grando SA: Programmed cell death of keratinocytes culminates in apoptotic secretion of a humectant upon secretagogue action of acetylcholine. J Cell Sci. 2001 Mar;114(Pt 6):1189-204. [PubMed
]
- Chia S, Megson IL, Ludlam CA, Fox KA, Newby DE: Preserved endothelial vasomotion and fibrinolytic function in patients with acute stent thrombosis or in-stent restenosis. Thromb Res. 2003;111(6):343-9. [PubMed
]
- Grando SA, Kist DA, Qi M, Dahl MV: Human keratinocytes synthesize, secrete, and degrade acetylcholine. J Invest Dermatol. 1993 Jul;101(1):32-6. [PubMed
]
- Beilin B, Bessler H, Papismedov L, Weinstock M, Shavit Y: Continuous physostigmine combined with morphine-based patient-controlled analgesia in the postoperative period. Acta Anaesthesiol Scand. 2005 Jan;49(1):78-84. [PubMed
]
- Tao J, Jin YF, Yang Z, Wang LC, Gao XR, Lui L, Ma H: Reduced arterial elasticity is associated with endothelial dysfunction in persons of advancing age: comparative study of noninvasive pulse wave analysis and laser Doppler blood flow measurement. Am J Hypertens. 2004 Aug;17(8):654-9. [PubMed
]
- Jiang JL, Jiang DJ, Tang YH, Li NS, Deng HW, Li YJ: Effect of simvastatin on endothelium-dependent vaso-relaxation and endogenous nitric oxide synthase inhibitor. Acta Pharmacol Sin. 2004 Jul;25(7):893-901. [PubMed
]
- Haug KH, Bogen IL, Osmundsen H, Walaas I, Fonnum F: Effects on cholinergic markers in rat brain and blood after short and prolonged administration of donepezil. Neurochem Res. 2005 Dec;30(12):1511-20. [PubMed
]
- Katoh H, Shimada T, Inoue S, Takahashi N, Shimizu H, Ohta Y, Nakamura K, Murakami Y, Ishibashi Y, Matsumori A: Reduced high serum hepatocyte growth factor levels after successful cardioversion in patients with atrial fibrillation. Clin Exp Pharmacol Physiol. 2004 Mar;31(3):145-51. [PubMed
]
- Main C, Blennerhassett P, Collins SM: Human recombinant interleukin 1 beta suppresses acetylcholine release from rat myenteric plexus. Gastroenterology. 1993 Jun;104(6):1648-54. [PubMed
]
- Ikarashi Y, Harigaya Y, Tomidokoro Y, Kanai M, Ikeda M, Matsubara E, Kawarabayashi T, Kuribara H, Younkin SG, Maruyama Y, Shoji M: Decreased level of brain acetylcholine and memory disturbance in APPsw mice. Neurobiol Aging. 2004 Apr;25(4):483-90. [PubMed
]
- Katz SD, Krum H: Acetylcholine-mediated vasodilation in the forearm circulation of patients with heart failure: indirect evidence for the role of endothelium-derived hyperpolarizing factor. Am J Cardiol. 2001 May 1;87(9):1089-92. [PubMed
]
- Hanna ST, Cao K, Wang R: Interaction of acetylcholine with Kir6.1 channels heterologously expressed in human embryonic kidney cells. Eur J Pharmacol. 2005 May 16;515(1-3):34-42. [PubMed
]
- Greig NH, Utsuki T, Ingram DK, Wang Y, Pepeu G, Scali C, Yu QS, Mamczarz J, Holloway HW, Giordano T, Chen D, Furukawa K, Sambamurti K, Brossi A, Lahiri DK: Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer beta-amyloid peptide in rodent. Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):17213-8. Epub 2005 Nov 7. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Choline O-acetyltransferase
- Acetylcholinesterase precursor
- Cholinesterase precursor
- Acetylcholinesterase
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5254 |
| Enzyme 1 Name |
Choline O-acetyltransferase |
| Enzyme 1 Synonyms |
- CHOACTase
- Choline acetylase
- ChAT
|
| Enzyme 1 Gene Name |
CHAT |
| Enzyme 1 Protein Sequence |
>Choline O-acetyltransferase
MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPH
PRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMA
AKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQ
QKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLIS
GVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPE
PEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSE
WAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANR
WYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQSSRKLIRADSVSELPAP
RRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQ
LAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLL
KDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQV
PTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRD
LCSLLPPTESKPLATKEKATRPSQGHQP
|
| Enzyme 1 Number of Residues |
748 |
| Enzyme 1 Molecular Weight |
82569 |
| Enzyme 1 Theoretical pI |
8.69 |
| Enzyme 1 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- acetyl-CoA + choline = CoA + O-acetylcholine
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
301096  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P28329  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
CLAT_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2247 bp
ATGGGGCTGAGGACAGCGAAGAAGAGGGGGCTTGGGGGAGGGGGGAAATGGAAGAGAGAG
GAGGGAGGAGGTACAAGAGGAAGGAGAGAAGTGCGGCCAGCTTGCTTTCTCCAGTCGGGT
GGCCGCGGGGACCCGGGCGACGTCGGAGGCCCTGCCGGGAACCCAGGCTGCAGCCCCCAC
CCCCGCGCTGCGACACGCCCCCCACCCCTTCCGGCTCACACCCCCGCCCACACTCCTGAG
TGGTGCGGTGCAGCGTCGGCCGAGGCAGCAGAGCCGAGGAGAGCAGGTCCACACCTCTGC
ATCCCTGCACCAGGACTCACCAAGACGCCCATCCTGGAAAAGGTCCCCCGTAAGATGGCA
GCAAAAACTCCCAGCAGTGAGGAGTCTGGGCTGCCCAAACTGCCCGTGCCCCCGCTGCAG
CAGACCCTGGCCACGTACCTGCAGTGCATGCGACACTTGGTGTCTGAGGAGCAGTTCAGG
AAGAGCCAGGCCATTGTGCAGCAGTTTGGGGCCCCTGGTGGCCTCGGCGAGACCCTGCAG
CAGAAACTCCTGGAGCGGCAGGAGAAGACAGCCAACTGGGTGTCTGAGTACTGGCTGAAT
GACATGTATCTCAACAACCGCCTGGCCCTGCCTGTCAACTCCAGCCCTGCCGTGATCTTT
GCTCGGCAGCACTTCCCTGGCACCGATGACCAGCTGAGGTTTGCAGCCAGCCTCATCTCT
GGTGTACTCAGCTACAAGGCCCTGCTGGACAGCCACTCCATTCCCACTGACTGTGCCAAA
CCGGAGCTGTCAGGGCAGCCCCTTTGCATGAAGCAATACTATGGGCTCTTCTCCTCCTAC
CGGCTCCCCGGCCATACCCAGGACACGCTGGTGGCTCAGAACAGCAGCATCATGCCGGAG
CCTGAGCACGTCATCGTAGCCTGCTGCAATCAGTTCTTTGTCTTGGATGTTGTCATTAAT
TTCCGCCGTCTCAGTGAGGGGGATCTGTTCACTCAGTTGAGAAAGATAGTCAAAATGGCT
TCCAACGAGGACGAGCGTTTGCCTCCAATTGGCCTGCTGACGTCTGACGGGAGGAGCGAG
TGGGCCGAGGCCAGGACGGTCCTCGTGAAAGACTCCACCAACCGGGACTCGCTGGACATG
ATTGAGCGCTGCATCTGCCTTGTATGCCTGGACGGCCCAGGAGGCGTGGAGCTCAGCGAC
ACCCACAGGGCACTCCAGCTCCTTCACGGCGGAGGCTACAGCAAGAACGGGGCCAATCGC
TGGTACGACAAGTCCCTGCAGTTTGTGGTGGGCCGAGACGCGACCTGCGGTGTGGTGTGC
GAACACTCCCCATTCGATGGCATCGTCCTGGTGCAGTGCACTGAGCATCTGCTCAAGCAC
ATGACGCAGAGCAGCAGGAAGCTGATCCGAGCAGACTCCGTCAGCGAGCTCCCCGCCCCC
CGGAGGCTGCGGTGGAAATGCTCCCCGGAAATTCAAGGCCACTTAGCCTCCTCGGCAGAA
AAACTTCAACGAATAGTAAAGAACCTTGACTTCATTGTCTATAAGTTTGACAACTATGGG
AAAACATTCATTAAGAAGCAGAAATGCAGCCCTGATGCCTTCATCCAGGTGGCCCTCCAG
CTGGCCTTCTACAGGCTCCACCGAAGACTGGTGCCCACCTACGAGAGCGCGTCCATCCGC
CGATTCCAGGAGGGACGCGTGGACAACATCAGATCGGCCACTCCAGAGGCACTGGCTTTT
GTGAGAGCCGTGACTGACCACAAGGCTGCTGTGCCAGCTTCTGAGAAGCTTCTGCTCCTG
AAGGATGCCATCCGTGCCCAGACTGCATACACAGTCATGGCCATAACAGGGATGGCCATT
GACAACCACCTGCTGGCACTGCGGGAGCTGGCCCGGGCCATGTGCAAGGAGCTGCCCGAG
ATGTTCATGGATGAAACCTACCTGATGAGCAACCGGTTTGTCCTCTCCACTAGCCAGGTG
CCCACAACCACGGAGATGTTCTGCTGCTATGGTCCTGTGGTCCCAAATGGGTATGGTGCC
TGCTACAACCCCCAGCCAGAGACCATCCTTTTCTGCATCTCTAGCTTTCACAGCTGCAAA
GAGACTTCTTCTAGCAAGTTTGCAAAAGCTGTGGAAGAAAGCCTCATTGACATGAGAGAC
CTCTGCAGTCTGCTGCCGCCTACTGAGAGCAAGCCATTGGCAACAAAGGAAAAAGCCACG
AGGCCCAGCCAGGGACACCAACCTTGA
|
| Enzyme 1 GenBank Gene ID |
S56138  |
| Enzyme 1 GeneCard ID |
CHAT  |
| Enzyme 1 GenAtlas ID |
CHAT  |
| Enzyme 1 HGNC ID |
HGNC:1912  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Oda Y, Nakanishi I, Deguchi T: A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. Brain Res Mol Brain Res. 1992 Dec;16(3-4):287-94. [PubMed
]
- Ohno K, Tsujino A, Brengman JM, Harper CM, Bajzer Z, Udd B, Beyring R, Robb S, Kirkham FJ, Engel AG: Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):2017-22. [PubMed
]
- Lorenzi MV, Trinidad AC, Zhang R, Strauss WL: Two mRNAs are transcribed from the human gene for choline acetyltransferase. DNA Cell Biol. 1992 Oct;11(8):593-603. [PubMed
]
- Toussaint JL, Geoffroy V, Schmitt M, Werner A, Garnier JM, Simoni P, Kempf J: Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. Genomics. 1992 Feb;12(2):412-6. [PubMed
]
- Cervini R, Rocchi M, DiDonato S, Finocchiaro G: Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. Neurosci Lett. 1991 Nov 11;132(2):191-4. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5772 |
| Enzyme 2 Name |
Acetylcholinesterase precursor |
| Enzyme 2 Synonyms |
- AChE
|
| Enzyme 2 Gene Name |
ACHE |
| Enzyme 2 Protein Sequence |
>Acetylcholinesterase precursor
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
|
| Enzyme 2 Number of Residues |
614 |
| Enzyme 2 Molecular Weight |
67797 |
| Enzyme 2 Theoretical pI |
6.24 |
| Enzyme 2 GO Classification |
| Function |
- carboxylic ester hydrolase activity
- catalytic activity
- cholinesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
Rapidly hydrolyzes choline released into the synapse |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- acetylcholine + H2O = choline + acetate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
177975  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P22303  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACES_HUMAN  |
| Enzyme 2 PDB ID |
1F8U  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1845 bp
ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC
CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG
GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC
TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA
CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC
TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC
CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA
TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC
TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG
AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC
AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC
TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG
GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC
GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG
CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG
GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG
CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT
GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT
GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC
AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG
GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG
GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC
CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC
TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC
GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG
AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC
AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG
TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC
GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG
GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC
CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA
|
| Enzyme 2 GenBank Gene ID |
M55040  |
| Enzyme 2 GeneCard ID |
ACHE  |
| Enzyme 2 GenAtlas ID |
ACHE  |
| Enzyme 2 HGNC ID |
HGNC:108  |
| Enzyme 2 Chromosome Location |
7 |
| Enzyme 2 Locus |
7q22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman-Hurwitz J, Lev-Lehman E, Ginzberg D, Lipidot-Lifson Y, et al.: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9688-92. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Wilson MD, Riemer C, Martindale DW, Schnupf P, Boright AP, Cheung TL, Hardy DM, Schwartz S, Scherer SW, Tsui LC, Miller W, Koop BF: Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. Nucleic Acids Res. 2001 Mar 15;29(6):1352-65. [PubMed
]
- Karpel R, Ben Aziz-Aloya R, Sternfeld M, Ehrlich G, Ginzberg D, Tarroni P, Clementi F, Zakut H, Soreq H: Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins. Exp Cell Res. 1994 Feb;210(2):268-77. [PubMed
]
- Chhajlani V, Derr D, Earles B, Schmell E, August T: Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. [PubMed
]
- Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A: The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. [PubMed
]
- Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. [PubMed
]
- Felder CE, Botti SA, Lifson S, Silman I, Sussman JL: External and internal electrostatic potentials of cholinesterase models. J Mol Graph Model. 1997 Oct;15(5):318-27, 335-7. [PubMed
]
- Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL: Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. [PubMed
]
- Bartels CF, Zelinski T, Lockridge O: Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet. 1993 May;52(5):928-36. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5774 |
| Enzyme 3 Name |
Cholinesterase precursor |
| Enzyme 3 Synonyms |
- Acylcholine acylhydrolase
- Choline esterase II
- Butyrylcholine esterase
- Pseudocholinesterase
|
| Enzyme 3 Gene Name |
BCHE |
| Enzyme 3 Protein Sequence |
>Cholinesterase precursor
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
|
| Enzyme 3 Number of Residues |
602 |
| Enzyme 3 Molecular Weight |
68419 |
| Enzyme 3 Theoretical pI |
7.47 |
| Enzyme 3 GO Classification |
| Function |
- carboxylic ester hydrolase activity
- catalytic activity
- cholinesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Lipid transport and metabolism |
| Enzyme 3 Specific Function |
An acylcholine + H(2)O = choline + a carboxylate |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- An acylcholine + H2O = choline + a carboxylate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1311630  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P06276  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CHLE_HUMAN  |
| Enzyme 3 PDB ID |
1P0Q  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1809 bp
ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC
ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA
GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC
TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG
TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT
TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT
TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG
ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT
CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA
TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG
TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA
ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA
AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG
GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC
TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT
CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG
ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT
AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT
GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA
GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT
TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT
GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG
GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA
TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA
AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA
AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC
TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG
AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG
ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT
TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG
GGTCTCTAA
|
| Enzyme 3 GenBank Gene ID |
M32391  |
| Enzyme 3 GeneCard ID |
BCHE  |
| Enzyme 3 GenAtlas ID |
BCHE  |
| Enzyme 3 HGNC ID |
HGNC:983  |
| Enzyme 3 Chromosome Location |
3 |
| Enzyme 3 Locus |
3q26.1-q26.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O: Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry. 1990 Jan 9;29(1):124-31. [PubMed
]
- Prody CA, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H: Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3555-9. [PubMed
]
- McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O: Brain cDNA clone for human cholinesterase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6682-6. [PubMed
]
- Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL: Complete amino acid sequence of human serum cholinesterase. J Biol Chem. 1987 Jan 15;262(2):549-57. [PubMed
]
- Lockridge O, Adkins S, La Du BN: Location of disulfide bonds within the sequence of human serum cholinesterase. J Biol Chem. 1987 Sep 25;262(27):12945-52. [PubMed
]
- Lockridge O: Structure of human serum cholinesterase. Bioessays. 1988 Oct;9(4):125-8. [PubMed
]
- McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN: Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc Natl Acad Sci U S A. 1989 Feb;86(3):953-7. [PubMed
]
- Iida S, Kinoshita M, Fujii H, Moriyama Y, Nakamura Y, Yura N, Moriwaki K: Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. Hum Mutat. 1995;6(4):349-51. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13052 |
| Enzyme 4 Name |
Acetylcholinesterase |
| Enzyme 4 Synonyms |
- YT blood group
- Acetylcholinesterase
- Yt blood group, isoform CRA_b
- cDNA FLJ77135, highly similar to Homo sapiens acetylcholinesterase
- YT blood group
- ACHE, transcript variant E4- E6, mRNA
|
| Enzyme 4 Gene Name |
ACHE |
| Enzyme 4 Protein Sequence |
>Acetylcholinesterase
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
|
| Enzyme 4 Number of Residues |
614 |
| Enzyme 4 Molecular Weight |
67797 |
| Enzyme 4 Theoretical pI |
6.24 |
| Enzyme 4 GO Classification |
| Function |
- carboxylic ester hydrolase activity
- catalytic activity
- cholinesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158256078  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A4D2E2  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A4D2E2_HUMAN  |
| Enzyme 4 PDB ID |
1F8U  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK291321  |
| Enzyme 4 GeneCard ID |
A4D2E2  |
| Enzyme 4 GenAtlas ID |
ACHE  |
| Enzyme 4 HGNC ID |
HGNC:108  |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |