EC - Dapdiamide synthase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
dapdiamide synthase
Other names:
3-[[[(2R,3R)-3-carboxyoxiran-2-yl]carbonyl]amino]-L-alanine—L-valine ligase
dapdiamide A synthase
Systematic name:
{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine:L-valine ligase (ADP-forming)



The enzyme, characterized from the bacterium Pantoea agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an (S)-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Hollenhorst, M. A., Clardy, J., Walsh, C. T.
    The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics.
    Biochemistry 48: 10467-10472 (2009). [PMID: 19807062]
  2. Hollenhorst, M. A., Bumpus, S. B., Matthews, M. L., Bollinger, J. M., Kelleher, N. L., Walsh, C. T.
    The nonribosomal peptide synthetase enzyme DdaD tethers N(beta)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/alpha-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis.
    J. Am. Chem. Soc. 132: 15773-15781 (2010). [PMID: 20945916]

[EC created 2015, modified 2016]