Literature summary for 2.6.1.44 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.

Search for more literature for 2.6.1.44

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermococcus litoralis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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
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 117, a small domain from residues 1847 and 295405 and a large domain of residues 48294. 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

Organism	UniProt	Comment	Textmining
Thermococcus litoralis	Q9C4M4	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermococcus litoralis
recombinant enzyme	Thermococcus litoralis

Synonyms

Synonyms	Comment	Organism
AGT	-	Thermococcus litoralis
alanine:glyoxylate aminotransferase	-	Thermococcus litoralis

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Release 2023.1 (January 2023)