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Literature summary for 6.3.2.8 extracted from

  • Shanmugam, A.; Natarajan, J.
    Comparative modeling of UDP-N-acetylmuramoyl-glycyl-D-glutamate-2,6-diaminopimelate ligase from Mycobacterium leprae and analysis of its binding features through molecular docking studies (2012), J. Mol. Model., 18, 115-125.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium leprae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-alanine Mycobacterium leprae
-
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium leprae P57994
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine Mur ligase reaction mechanism, overview Mycobacterium leprae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-alanine
-
Mycobacterium leprae ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
?

Subunits

Subunits Comment Organism
More MurC domain structure and three-dimensional structure modeling by homology modeling method, structure comparisons of Mur ligases, overview Mycobacterium leprae

Synonyms

Synonyms Comment Organism
MurC
-
Mycobacterium leprae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mycobacterium leprae

General Information

General Information Comment Organism
additional information MurC substrate binding site structures and three-dimensional structure modeling by homology modeling method, structure comparisons of Mur ligases, detailed overview. Identification of residues playing an important role in the catalytic activity of each of the Mur enzymes, docking of enzyme and substrate and ATP Mycobacterium leprae