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Literature summary for 2.6.1.88 extracted from

  • Dolzan, M.; Johansson, K.; Roig-Zamboni, V.; Campanacci, V.; Tegoni, M.; Schneider, G.; Cambillau, C.
    Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function (2004), FEBS Lett., 571, 141-146.
    View publication on PubMed
Search for more literature for 2.6.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C41 (DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 0.2 M NaCl, 0.1 M sodium/potassium phosphate, pH 6.3, and 23.5% (w/v) PEG1000, at 20°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45647
-
 2 * 45647, X-ray crystallography Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77806
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+ affinity column chromatography and Superdex 200 pg gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidine + a 2-oxo acid 88% activity compared to L-methionine (at 1 mM) Escherichia coli ?
-
 ?
L-leucine + a 2-oxo acid 11% activity compared to L-methionine (at 1 mM) Escherichia coli ?
-
 ?
L-methionine + a 2-oxo acid the enzyme shows a preference for L-methionine (100% activity at 1 mM L-methionine) Escherichia coli ?
-
 ?
L-phenylalanine + a 2-oxo acid 57% activity compared to L-methionine (at 1 mM) Escherichia coli ?
-
 ?
L-tyrosine + a 2-oxo acid 9% activity compared to L-methionine (at 1 mM) Escherichia coli ?
-
 ?
additional information the enzyme does not use L-tryptophan, L-valine, L-asparagine, L-glutamate, and L-arginine as substrates Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 45647, X-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
methionine aminotransferase
-
 Escherichia coli
YbdL
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on. The active site contains a bound pyridoxal 5'-phosphate, covalently attached to the conserved active site lysine residue Lys236 Escherichia coli