KEGG   ENZYME: 6.3.2.47Help
Entry
EC 6.3.2.47                 Enzyme                                 

Name
dapdiamide synthase;
DdaF;
dapdiamide A synthase
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine:L-valine ligase (ADP-forming)
Reaction(IUBMB)
(1) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-valine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-valine [RN:R10942];
(2) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-isoleucine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-isoleucine [RN:R10943];
(3) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-leucine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-leucine [RN:R10944];
(4) ATP + 3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanine + L-valine = ADP + phosphate + 3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanyl-L-valine [RN:R10941]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine [CPD:C20966];
L-valine [CPD:C00183];
L-isoleucine [CPD:C00407];
L-leucine [CPD:C00123];
3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanine [CPD:C20967]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-valine [CPD:C20962];
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-isoleucine [CPD:C20963];
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-leucine [CPD:C20964];
3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanyl-L-valine [CPD:C20965]
Comment
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.
History
EC 6.3.2.47 created 2015, modified 2016
Reference
1  [PMID:19807062]
  Authors
Hollenhorst MA, Clardy J, Walsh CT
  Title
The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics.
  Journal
Biochemistry. 48 (2009) 10467-72.
  Sequence
Reference
2  [PMID:20945916]
  Authors
Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM Jr, Kelleher NL, Walsh CT
  Title
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.
  Journal
J. Am. Chem. Soc. 132 (2010) 15773-81.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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