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2.3.1.5: arylamine N-acetyltransferase

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

Word Map on EC 2.3.1.5

Reaction

acetyl-CoA
+
an arylamine
=
CoA
 +
an N-acetylarylamine

Synonyms

(BACAN)NAT3, (MYCAB)NAT1, 2-naphthylamine N-acetyltransferase, 4-aminobiphenyl N-acetyltransferase, ABW01_24350, acetyl CoA-arylamine N-acetyltransferase, acetyltransferase, 2-naphthylamine N-, acetyltransferase, 4-aminobiphenyl, acetyltransferase, arylamine, acetyltransferase, p-aminosalicylate N-, acetyltransferase, procainamide N-, acetyltransferase, serotonin N-, arylamine acetylase, arylamine acetyltransferase, arylamine N-acetyl transferase, arylamine N-acetyltransferase, arylamine N-acetyltransferase 1, arylamine N-acetyltransferase 2, arylamine N-acetyltransferase C, arylamine N-acetyltransferase I, arylamine N-acetyltransferase type 1, arylamine N-acetyltransferase type 2, arylamine N-acetyltransferase type I, arylamine-N-acetyltransferase 1, BanatA, BanatB, BanatC, beta-naphthylamine N-acetyltransferase, indoleamine N-acetyltransferase, MlNAT1, MMNAT, More, MSNAT, N-acetyltransferase, N-acetyltransferase a, N-acetyltransferase b, N-acetyltransferase type 2, N-hydroxyarylamine O-acetyltransferase, NAT, NAT 1, NAT-a, NAT-b, NAT1, NAT2, NAT2*1, NAT2*2, NAT3, NAT31, NfNAT, p-aminosalicylate N-acetyltransferase, PANAT, rhesus NAT2, serotonin acetyltransferase, serotonin N-acetyltransferase, STNAT, TBNAT, Tpau_4046, UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid 3-N-acetyltransferase, UDP-D-Glc(2NAc3N)A 3-N-acetyltransferase, WbpD

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.5 arylamine N-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.5 - arylamine N-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of mutant Y183F is reported
-
crystals diffract to 1.95 A resolution on a synchrotron source
-
in complex with coenzyme A
Q81R98
hanging drop vapor diffusion method, using 1.6 M sodium citrate, pH 6.5, 0.28 M NDSB-221 as additive
-
high resolution crystal structures of both human NATs, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a site-directed NAT1 mutant, NAT1-F125S, and a NAT2-CoA complex are presented. By comparing the structures with known prokaryotic structures, evidences are provided for novel structural features of human NATs that are absent in bacterial enzymes, including an insertion that produces a significant difference in the structure of the carboxyl terminus of the eukaryotic enzymes
-
high resolution crystal structures of both human NATs, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a site-directed NAT1 mutant, NAT1-F125S, and a NAT2-CoA complex are presented. By comparing the structures with known prokaryotic structures, evidences are provided for novel structural features of human NATs that are absent in bacterial enzymes, including an insertion that produces a significant difference in the structure of the carboxyl terminus of the eukaryotic enzymes. A complete picture of the distinct substrate selectivity of human NAT1 and NAT2, as well as key features of the naturally occurring variants of NAT1 and NAT2 is provided
-
in complex with 2-bromoacetanilide
in complex with coenzyme A
modelling predicts that ATP binds within the active site cleft arranged with the triphosphate group in close proximity to arginine 127
the regions spanning N177-L180 and D285-F288, possess inherent motions on the nanosecond time scale. The latter segment becomes more restricted in its motions upon substrate binding. Data suggest that NAT acetylation may protect the enzyme from ubiquitination
-
crystallization in 0.5 M Ca(OAc)2, 16% PEG 3350, and 0.1 M Tris-HCl, pH 8.5, sitting drop vapor-diffusion method
-
in complex with CoA, sitting drop vapor diffusion method, using 20% (w/v) PEG 4000, 0.6 M NaCl, 0.1 M MES buffer pH 6.5
crystal structure of MMNAT in complex with CoA is determined. The overall MMNAT structure consists of three domains. Domain I forms an alpha-helical bundle (amino acids 4-88), domain II forms a beta-barrel (amino acids 89-200) and domain III forms an alpha/beta lid (amino acids 201-275). Assembled together, the molecular surface of these domains presents a deep and wide active-site cleft, at the base of which is found the catalytic cysteine residue. Surprisingly, the principal CoA recognition site in MMNAT is located some 30 A from the site of CoA recognition in the deposited structure of human NAT2 bound to CoA
-
Mycobacterium smegmatis and Mycobacterium marinum
-
the crystal structure of the native enzyme is presented at a resolution of 1.9 A, cocrystallized with CoA at 2.4 A
-
sitting drop vapor diffusion method, using either 0.2 M MgCl2 or 0.2 M CaCl2, in 0.1 M HEPES pH 7.0, with 20% (w/v) PEG 6000
vapor diffusion method, using 15% (w/v) PEG 6000, 5% (v/v) glycerol at 18°C
-
Mycobacterium smegmatis and Mycobacterium marinum
crystal structure of NfNAT is solved at a resolution of 2.7 A. Despite low sequence identity, enzyme shares an almost identical fold with that of other prokaryotic NATs, e.g. Mycobacterium smegmatis NAT and Mycobacterium marinum NAT. The overall NfNAT structure consists of three domains of equivalent size. The first two domains, a helical bundle (amino acids 1-98) and a beta-barrel (amino acids 99-199), are disposed in such a way that three residues (Cys82, His119, and Asp136) form a catalytic triad. The third domain is linked to the second through an interdomain helix (alpha6: amino acids 200-210). As shown for other prokaryotic NAT structures, the interface formed between domains 2 and 3 forms a substantial active-site cleft
the structure of NfNAT is solved at a resolution of 2.7 A
hanging- and sitting-drop vapour diffusion method
-