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2.3.1.35: glutamate N-acetyltransferase

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

Word Map on EC 2.3.1.35

Reaction

N2-Acetyl-L-ornithine
+
L-glutamate
=
L-ornithine
 +
N-acetyl-L-glutamate

Synonyms

acetylglutamate synthetase, acetylglutamate-acetylornithine transacetylase, acetylglutamic synthetase, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, acetyltransferase, glutamate, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, argJ, CcOATase, CLGAT, glutamate acetyltransferase, glutamate N-acetyltransferase, L-ornithine acetyltransferase, Mtb OAT, N-acetyl-L-glutamate synthetase, OAT, OAT2, OATase, ornithine acetyl transferase, ornithine acetyltransferase, ornithine transacetylase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.35 glutamate N-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.35 - glutamate N-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of Mtb OAT in native form and in its complex with ornithine has been determined at 1.7 and 2.4 A resolutions, respectively. Ornithine binding does not alter the structure of Mtb OAT globally. Its presence stabilizes the three C-terminal residues that are disordered and not observed in the native structure. Stabilization of the C-terminal residues by ornithine reduces the size of the active-site pocket volume in the structure of the ORN complex. The interactions of ORN and the protein residues of Mtb OAT unambiguously delineate the active-site residues of this enzyme in Mtb.
diffraction to 1.7 A resolution, space group P212121
crystals grown by either the batch or hanging-drop vapour-diffusion method. The crystals belong to space group P4, with unit-cell parameters a = b = 66.98, c = 427.09 A. The use of the counterdiffusion technique is critical for the production of well ordered crystals
-
crystallization of OAT2 in the presence of N-alpha-acetyl-L-glutamate leads to a structure in which residue T181 is acetylated, the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures. The two acyl-enzyme complex structures can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181
crystals of OAT2 in complex with L-Glu are generated. Optimization of crystallization conditions lead to a 2.7 A resolution structure for OAT2 acylated at Thr-181 and in complex with L-Glu (referred to as the acetyl-OAT2-glutamate complex)
purified recombinant native and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, 12 mg/ml protein in 1.1-1.3 M ammonium sulfate, 0.04 M ammonium phosphate, 0.1 M Tris-HCl, pH 8.0, and 5-8% v/v glycerol, and in case of SeMet-enzyme 5 mM DTT, cryoprotection by 25% glycerol and 2.0 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.8 A resolution