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2.6.1.62: adenosylmethionine-8-amino-7-oxononanoate transaminase

This is an abbreviated version!
For detailed information about adenosylmethionine-8-amino-7-oxononanoate transaminase, go to the full flat file.

Word Map on EC 2.6.1.62

Reaction

S-adenosyl-L-methionine
+
8-Amino-7-oxononanoate
=
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate
 +
7,8-diaminononanoate

Synonyms

7,8-diaminononanoate transaminase, 7,8-diaminopelargonate synthase, 7,8-diaminopelargonic acid aminotransferase, 7,8-diaminopelargonic acid synthase, 7,8-diaminopelargonic acid transaminase, 7,8-diaminoperlargonic acid aminotransferase, 7-keto-8-aminopelargonic acid aminotransferase, 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase, Bio3-Bio1, bioA, DAPA amino transferase, DAPA aminotransferase, DAPA AT, DAPA synthase, DAPA transaminase, diaminopelargonate synthase, diaminopelargonic acid transaminase, diaminoperlargonic acid aminotransferase, More, NCgl2515, Pcryo_0361, S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase, synthase, diaminopelargonate

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.62 adenosylmethionine-8-amino-7-oxononanoate transaminase

Crystallization

Crystallization on EC 2.6.1.62 - adenosylmethionine-8-amino-7-oxononanoate transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the native and the selenomethionine enzyme, without ligand in two different space groups. In both cases, the structures show a dimer made of two monomers related by a noncrystallographic twofold axis
native and the selenomethionine enzyme without ligand, in two different space groups. The structures show a dimer made of two monomers related by a noncrystallographic twofold axis
complex of holoenzyme and 7-keto-8-aminopelargonic acid
-
hanging drop vapor diffusion method
-
purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20°C, 10 mg/ml protein in solution mixed with equal volume of well solution containing 26-28% PEG 4000, 9-12% methylpentanediol, 100 mM HEPES, pH 7.5, microseeding, 2 days, X-ray diffraction structure determination and analysis at 1.7-2.4 A resolution, modeling
in complex with inhibitors 5-(pyridin-2-yl)thiophene-2-carboxamide, 4-(1H-imidazol-1-yl)benzamide, and N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine
in complex with substrate 7-oxo-8-aminopelargonic acid and in complex with inhibitors 1-(1,3-benzothiazol-2-yl)methanamine and 2-hydrazinyl-1,3-benzothiazole. The side chains of Tyr25, Trp65, Arg400, and Tyr407 are shown to be quite flexible. Small molecule binding induces unexpected conformational remodeling in the substrate binding site
to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 11 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.02 mM PLP, pH 7.9, with precipitant solution containing 0.1 M sodium citrate, pH 6.1, 0.2 M potassium sodium tartrate, and 1.8 M ammonium sulfate. A glass capillary containing 0.008 ml of protein solution is mounted in the gel tube with 1% agarose presoaked in 1 ml of the precipitant solution, method optimization, 1 month at 20°C. X-ray diffraction structure determination and analysis at 1.6 A resolution