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Literature summary for 2.6.1.83 extracted from

  • Sobolev, V.; Edelman, M.; Dym, O.; Unger, T.; Albeck, S.; Kirma, M.; Galili, G.
    Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis (2013), Acta Crystallogr. Sect. F, 69, 84-89.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged protein (amino acid residue 21-456) expressed in Escherichia coli BL21(DE3) Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
PEG 3350 Arabidopsis thaliana
to 2.3 A resolution. The large donain (Pro85–Ser338) consists of 254 residues and has an alpha-beta-alpha sandwich fold. The large domain includes both the pyridoxal phosphate-binding site and the dimerization site. The small domain is composed of the remaining residues, Gly34–Ile84 and Ser339–Thr441. The small domain has an alpha/beta architecture, with a beta-sheet surrounded by two outer layers alpha-helices Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9ZQI7
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal ion affinity chromatography (Ni2+), gel filtration Arabidopsis thaliana

Subunits

Subunits Comment Organism
homodimer gel filtration Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
Ald1
-
Arabidopsis thaliana
diaminopimelate aminotransferase
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Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Arabidopsis thaliana