KEGG   ENZYME: 6.3.2.47
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)
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
Pathway
ec00998  Biosynthesis of various antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K22114  dapdiamide synthase
Genes
SPESpro_0344
SPLYQ5A_016905(purD_2)
PVAPvag_pPag20162 Pvag_pPag20163
PAGCBEE12_22710
PPEEI6G31_07780
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 48:10467-72 (2009)
DOI:10.1021/bi9013165
  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 132:15773-81 (2010)
DOI:10.1021/ja1072367
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.47
IUBMB Enzyme Nomenclature: 6.3.2.47
ExPASy - ENZYME nomenclature database: 6.3.2.47
BRENDA, the Enzyme Database: 6.3.2.47

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