Sequence of SNAT_SHEEP
EC Number:2.3.1.87
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
Other sequences found for EC No. 2.3.1.87
General information:
Sequence
0 MSTPSVHCLK PSPLHLPSGI PGSPGRQRRH TLPANEFRCL TPEDAAGVFE IEREAFISVS
60 GNCPLNLDEV QHFLTLCPEL SLGWFVEGRL VAFIIGSLWD EERLTQESLA LHRPRGHSAH
120 LHALAVHRSF RQQGKGSVLL WRYLHHVGAQ PAVRRAVLMC EDALVPFYQR FGFHPAGPCA
180 IVVGSLTFTE MHCSLRGHAA LRRNSDR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1126302
Coon S.L.,Roseboom P.H.,Baler R.,Weller J.L.,Namboodiri M.A.A.,Koonin E.V.,Klein D.C.
Pineal serotonin N-acetyltransferase: expression cloning and molecular analysis.
Science
270
1681-1683
1995
1126303
Coon S.L.,Weller J.L.,Korf H.-W.,Namboodiri M.A.,Rollag M.,Klein D.C.
cAMP regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation.
J. Biol. Chem.
276
24097-24107
2001
1126304
Ganguly S.,Gastel J.A.,Weller J.L.,Schwartz C.,Jaffe H.,Namboodiri M.A.,Coon S.L.,Hickman A.B.,Rollag M.,Obsil T.,Beauverger P.,Ferry G.,Boutin J.A.,Klein D.C.
Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis.
Proc. Natl. Acad. Sci. U.S.A.
98
8083-8088
2001
1126306
Zheng W.,Zhang Z.,Ganguly S.,Weller J.L.,Klein D.C.,Cole P.A.
Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation.
Nat. Struct. Biol.
10
1054-1057
2003
1126307
Ganguly S.,Weller J.L.,Ho A.,Chemineau P.,Malpaux B.,Klein D.C.
Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205.
Proc. Natl. Acad. Sci. U.S.A.
102
1222-1227
2005
1126308
Pavlicek J.,Coon S.L.,Ganguly S.,Weller J.L.,Hassan S.A.,Sackett D.L.,Klein D.C.
Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87).
J. Biol. Chem.
283
14552-14558
2008
1126309
Hickman A.B.,Namboodiri M.A.,Klein D.C.,Dyda F.
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.
Cell
97
361-369
1999
1126310
Hickman A.B.,Klein D.C.,Dyda F.
Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism.
Mol. Cell
3
23-32
1999
1126311
Obsil T.,Ghirlando R.,Klein D.C.,Ganguly S.,Dyda F.
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.
Cell
105
257-267
2001
1126312
Scheibner K.A.,De Angelis J.,Burley S.K.,Cole P.A.
Investigation of the roles of catalytic residues in serotonin N-acetyltransferase.
J. Biol. Chem.
277
18118-18126
2002
1126313
Wolf E.,De Angelis J.,Khalil E.M.,Cole P.A.,Burley S.K.
X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition.
J. Mol. Biol.
317
215-224
2002
