Entry Name dapdiamide synthase;
Class Ligases;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
Pathway ec00998 Biosynthesis of various antibiotics
ec01110 Biosynthesis of secondary metabolites
Orthology Genes PVA : Pvag_pPag20162 Pvag_pPag20163
Taxonomy Reference 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 Sequence Reference 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 Sequence Other DBs ExplorEnz - The Enzyme Database: 6.3.2.47
ExPASy - ENZYME nomenclature database: 6.3.2.47
LinkDB All DBs
