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Information on EC 2.6.1.83 - LL-diaminopimelate aminotransferase and Organism(s) Chlamydia trachomatis and UniProt Accession O84395

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.83 LL-diaminopimelate aminotransferase
IUBMB Comments
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
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Chlamydia trachomatis
UNIPROT: O84395
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Word Map
The taxonomic range for the selected organisms is: Chlamydia trachomatis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ll-dap-at, atdap-at, l,l-diaminopimelate aminotransferase, ctdap-at, ll-diaminopimelate aminotransferase, diaminopimelate aminotransferase, vsdapl, ct390, ll-dap aminotransferase, sll0480, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LL-DAP aminotransferase
-
LL-diaminopimelate aminotransferase
-
LL-diaminopimelate aminotransferase
-
-
SYSTEMATIC NAME
IUBMB Comments
LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
show the reaction diagram
-
-
-
?
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
show the reaction diagram
-
-
-
?
meso-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
show the reaction diagram
-
-
-
?
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
show the reaction diagram
-
also active (17%-21%) with lysine, L-ornithine and cystathionine
-
-
r
meso-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-bis((7-chloro-4-quinolinyl)amino)-2-propanol
-
NSC_5485, potential drug candidate that can inhibit the enzymatic activity of enzyme CtDAP-AT
additional information
-
high-throughput virtual screening for potential enzyme inhibitors using the optimized and corrected PLP-bound L,Ldiaminopimelate aminotransferase structure based on the crystal structure, PDB ID 3ASB. Comparative molecular dynamics simulation studies of enzyme CtDAP-AT in apoform and in complex with potential inhibitors, intermolecular interaction profiling of the compounds in complex with CtDAP-AT
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
crystal structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion methodPEG 6000
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA chemically synthesized, His-tagged protein expressed in Escherichia coli M15(pREP4) and Escherichia coli BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a target for drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hudson, A.O.; Gilvarg, C.; Leustek, T.
Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase
J. Bacteriol.
190
3256-3263
2008
Syntrophobacter fumaroxidans (A0LEA5), Methanothermobacter thermautotrophicus (O26158), Aquifex aeolicus (O66630), Chlamydia trachomatis (O84395), Desulfitobacterium hafniense (Q18T09), Methanosphaera stadtmanae (Q2NFU1), Moorella thermoacetica (Q2RK33), Trichormus variabilis (Q3MAL4), Trichormus variabilis (Q3MDN5), Synechocystis sp. (Q55828), Bacteroides fragilis (Q5LC03), Candidatus Protochlamydia amoebophila (Q6MDE0), Leptospira interrogans (Q72NJ3), Geobacter sulfurreducens (Q74GT3), Gloeobacter violaceus (Q7NDX4), Methanosarcina acetivorans (Q8TQ40)
Manually annotated by BRENDA team
Watanabe, N.; James, M.N.
Structural insights for the substrate recognition mechanism of LL-diaminopimelate aminotransferase
Biochim. Biophys. Acta
1814
1528-1533
2011
Arabidopsis thaliana, Chlamydia trachomatis
Manually annotated by BRENDA team
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
J. Mol. Biol.
411
649-660
2011
Chlamydia trachomatis (O84395), Chlamydia trachomatis
Manually annotated by BRENDA team
Sadhasivam, A.; Vetrivel, U.
Identification of potential drugs targeting L,L-diaminopimelate aminotransferase of Chlamydia trachomatis an integrative pharmacoinformatics approach
J. Cell. Biochem.
120
2271-2288
2019
Chlamydia trachomatis
Manually annotated by BRENDA team