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2.3.1.87: aralkylamine N-acetyltransferase

This is an abbreviated version!
For detailed information about aralkylamine N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.87

Reaction

acetyl-CoA
+
a 2-arylethylamine
=
CoA
 +
an N-acetyl-2-arylethylamine

Synonyms

AA-NAT, AANAT, AANAT1, AANAT2, AANAT3, AANATL7, AATNATL2, acetyl-CoA:aralkylamine N-acetyltransferase, acetyltransferase, arylalkylamine N-, arylalkylamine N-acetyltransferase, arylalkylamine N-acetyltransferase 1, arylalkylamine N-acetyltransferase 1a, arylalkylamine N-acetyltransferase 1b, arylalkylamine N-acetyltransferase 2, arylalkylamine N-acetyltransferase like 7, arylalkylamine N-acetyltransferase-2, Bm-iAANAT, Eis, hAANAT, More, MSMEG_3513, N-acetyltransferase, NAT, oAANAT, PA4534, PaaNAT, Rv2416c, serotonin acetylase, serotonin acetyltransferase, serotonin N-acetyltransferase, serotonin-N-acetyltransferase, SNA, SNAT, SNAT1, SNAT2

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.87 aralkylamine N-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.87 - aralkylamine N-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, mixing of 0.001 ml of both protein and reservoir solution, equilibration against 0.15 ml of reservoir solution containing 0.17 M ammonium acetate, 25.5% PEG 4000, and 17% glycerol, and 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis, molecular replacement, modeling
solution NMR studies. AANAT3 is well-folded in solution. The P-loop, which is responsible for cofactor binding, is flexible in the free-state, while a large region of the enzyme interconverts between two distinct conformations in the slow exchange regime
-
molecular modeling, docking of N-acetylserotonin and screening for potential ligands. N-[2-(5-hydroxy-1H-indol-3-yl)ethy1]-3-(4-hydroxyphenyl)-2-propenamide show least binding energy, i.e. -9.38 Kcal/mol
structure of apoenzyme and in complex with acetyl-CoA, to 2.21 and 1.65 A resolution, respectively. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel