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Literature summary extracted from

  • Watanabe, N.; Clay, M.D.; van Belkum, M.J.; Fan, C.; Vederas, J.C.; James, M.N.
    The structure of LL-diaminopimelate aminotransferase from Chlamydia trachomatis: implications for its broad substrate specificity (2011), J. Mol. Biol., 411, 649-660.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.83 DNA chemically synthesized, His-tagged protein expressed in Escherichia coli M15(pREP4) and Escherichia coli BL21(DE3) Chlamydia trachomatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.83 sitting-drop vapor diffusion methodPEG 6000 Chlamydia trachomatis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.83 Chlamydia trachomatis O84395
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.83 immobilized metal ion affinity chromatography Chlamydia trachomatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.83 LL-diaminopimelate + 2-oxoglutarate
-
 Chlamydia trachomatis L-glutamate + tetrahydrodipicolinate + H2O
-
 ?
2.6.1.83 meso-diaminopimelate + 2-oxoglutarate
-
 Chlamydia trachomatis L-glutamate + tetrahydrodipicolinate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.83 homodimer crystal structure analysis Chlamydia trachomatis

Synonyms

EC Number Synonyms Comment Organism
2.6.1.83 LL-diaminopimelate aminotransferase
-
 Chlamydia trachomatis

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.83 pyridoxal 5'-phosphate
-
 Chlamydia trachomatis