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Literature summary extracted from

  • Sakuraba, H.; Yoneda, K.; Takeuchi, K.; Tsuge, H.; Katunuma, N.; Ohshima, T.
    Structure of an archaeal alanine:glyoxylate aminotransferase (2008), Acta Crystallogr. Sect. D, 64, 696-699.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.44 expression in Escherichia coli Thermococcus litoralis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.44 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 Thermococcus litoralis
2.6.1.44 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 Thermococcus litoralis
2.6.1.44 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 Thermococcus litoralis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.44 Thermococcus litoralis Q9C4M4
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.44
-
 Thermococcus litoralis
2.6.1.44 recombinant enzyme Thermococcus litoralis

Synonyms

EC Number Synonyms Comment Organism
2.6.1.44 AGT
-
 Thermococcus litoralis
2.6.1.44 alanine:glyoxylate aminotransferase
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 Thermococcus litoralis