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Literature summary for 2.6.1.83 extracted from

  • Adams, L.E.; Rynkiewicz, P.; Babbitt, G.A.; Mortensen, J.S.; North, R.A.; Dobson, R.C.J.; Hudson, A.O.
    Comparative molecular dynamics simulations provide insight into antibiotic interactions a case study using the enzyme L,L-diaminopimelate aminotransferase (DapL) (2020), Front. Mol. Biosci., 7, 46 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.83

Application

Application Comment Organism
drug development the LL-diaminopimelate aminotransferase (DapL) pathway is an attractive pipeline to identify targets for the development of antibiotic compounds Verrucomicrobium spinosum

Inhibitors

Inhibitors Comment Organism Structure
Barbiturate binding structure model Verrucomicrobium spinosum
hydrazide binding structure model Verrucomicrobium spinosum
additional information rhodanine, barbiturate, hydrazide, and thiobarbiturate associations with VsDapL are supported by molecular dynamics simulations, docking study, overview Verrucomicrobium spinosum
rhodanine binding structure model Verrucomicrobium spinosum
thiobarbiturate binding structure model Verrucomicrobium spinosum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
LL-2,6-diaminoheptanedioate + 2-oxoglutarate Verrucomicrobium spinosum
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 (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Verrucomicrobium spinosum A0A6P3CW87
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
-
 Verrucomicrobium spinosum (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
 r

Subunits

Subunits Comment Organism
homodimer
-
 Verrucomicrobium spinosum

Synonyms

Synonyms Comment Organism
DapL
-
 Verrucomicrobium spinosum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Verrucomicrobium spinosum

General Information

General Information Comment Organism
metabolism the LL-diaminopimelate aminotransferase (DapL) pathway is a variant of the lysine biosynthetic pathway, overview Verrucomicrobium spinosum
additional information comparative molecular dynamics simulations, ligand docking study, sequence comaprisons and three-dimensional homology modelling, active site structure, detailed overview. Key conserved active site residues are identified as I43, G44, Y74, E77, K111, Y134, N189, K251, N294, and R390 Verrucomicrobium spinosum
physiological function DapL is a homodimer that catalyzes the conversion of tetrahydrodipicolinate to LL-diaminopimelate in a single transamination reaction. The penultimate and ultimate products of the lysine biosynthesis pathway, meso-diaminopimelate and lysine, are key components of the Gram-negative and Gram-positive bacterial peptidoglycan cell wall Verrucomicrobium spinosum