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2.6.1.44: alanine-glyoxylate transaminase

This is an abbreviated version!
For detailed information about alanine-glyoxylate transaminase, go to the full flat file.

Word Map on EC 2.6.1.44

Reaction

L-alanine
+
glyoxylate
=
pyruvate
 +
glycine

Synonyms

3-hydroxykynurenine transaminase, 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase, AGT, AGT-Ma, AGT-Mi, AGT1, AGT2, AGX, AGXT, AGXT2, alanine aminotransferase, alanine glyoxalate transaminase 2, alanine glyoxylate aminotransferase, alanine-glyoxalate aminotransferase, alanine-glyoxalate transaminase 1, alanine-glyoxylate aminotransferase, alanine-glyoxylate aminotransferase 2, alanine-glyoxylate aminotransferase isoenzyme 2, alanine-glyoxylate aminotransferase-2, alanine-glyoxylic aminotransferase, alanine: glyoxylate aminotransferase, alanine:2-oxoglutarate aminotransferase, alanine:glyoxylate aminotransferase, alanine:glyoxylate aminotransferase 1, alanine:glyoxylate aminotransferase 2, alanine:glyoxylate aminotransferase type 1, alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase, aminotransferase 3, AT3, At3g08860, cytosolic alanine aminotransferase, D-AIB AT, EC 2.6.1.51, GGT, glyoxylate aminotransferase AGT1, L-alanine-glycine transaminase, L-alanine-glyoxylate aminotransferase, L-alanine:glyoxylate aminotransferase, More, serine pyruvate aminotransferase, serine:pyruvate/alanine:glyoxylate aminotransferase, SPT/AGT

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.44 alanine-glyoxylate transaminase

Crystallization

Crystallization on EC 2.6.1.44 - alanine-glyoxylate transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 12% polyethylene glycol 8000, 0.13 M magnesium acetate, 4% butanol, and 0.1 M cacodylic acid at pH 6.5
-
enzyme in apoform and complexed with L-serine, large, greenish-yellow crystals grow from drops containing equal volumes of 11 mg/ml protein in 0.2 mM PLP, 10% glycerol, and 100 mM Tris-HCl, pH 8.5, and precipitant solution containing 4.1-4.2 M sodium formate, equilibration against the same precipitant, several days, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.1 A resolution, respectively, modelling
crystals belong to space group P4(1)2(1)2 or its enantiomorph with uni-cell parameters a = b = 90.81, c = 142.62 A
-
mutant S187F, to a resolution of 2.9 A. The overall conformation of the variant is similar to that of normal AGTwith a displacement of the PLP-binding Lys209 and Val185, located on the re and si side of PLP, respectively, and slight conformational changes of other active site residues, in particular Trp108, the base stacking residue with the pyridine cofactor moiety. This results in a mispositioning of the AGT-pyridoxamine 5'-phosphate complex and of the external aldimine
purified recombinant wild-type enzyme in complex with inhibitors L- and D-cycloserine (LCS and DCS), hanging drop vapor diffusion technique, mixing of 0.001 ml of protein/ligand solution containing 0.215 mM enzyme, 2 mM DCS, and 50 mM potassium phosphate, pH 7.4, with an equal volume of reservoir solution containing 10-12% PEG 6000, 5% 2-methyl-2,4-pentanediol (MPD), and 0.1 M MES, pH 6.5, single crystals are cryoprotected by fast soaking into a reservoir solution containing 2 mM DCS and 25% MPD, for the AGT-LCS complex, AGT native crystals grown in the described conditions, with the exception of DCS, are soaked into a solution containing the reservoir and 20 mM LCS and 20% MPD, X-ray diffraction structure determination and analysis at 2.7-3.0 A resolution, modelling
using 10% (w/v) PEG 4000 in 0.1 M Na HEPES pH 7.5
crystallization of the native and selenomethionyl alanine:glyoxylate aminotransferase is performed using the hanging-drop vapour-diffusion method. Crystal struture is determined at 2.3 A resolution
crystallization of the native and selenomethionyl enzyme is performed using the hanging-drop vapour-diffusion method. Crystal structure is determined at 2.3 A resolution
native enzyme and selenomethionine derivative, to 2.3 A and 2.55 A resolution, respectively. Enzyme is a tetramer. The monomer consists of an N-terminal arm of residues 1–17, a small domain from residues 18–47 and 295–405 and a large domain of residues 48–294. The amino-acid residues involved in cofactor binding are Asn175, Tyr206, Lys234 and Arg242. The guanidino group of Arg361 forms a salt bridge with one carboxylate of the maleate, Thr108 forms a salt bridge with the side-chain carboxylate of the maleate