Entry
Name
fumarate---(S)-2,3-diaminopropanoate ligase;
DdaG;
fumarate:(S)-2,3-diaminopropanoate ligase (AMP-forming)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
fumarate:L-2,3-diaminopropanoate ligase (AMP-forming)
Reaction(IUBMB)
ATP + fumarate + L-2,3-diaminopropanoate = AMP + diphosphate + N3-fumaroyl-L-2,3-diaminopropanoate [RN:
R10940 ]
Reaction(KEGG)
Substrate
Product
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ];
N3-fumaroyl-L-2,3-diaminopropanoate [CPD:
C20961 ]
Comment
The enzyme, characterized from the bacterium Enterobacter agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an L-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold.
History
EC 6.3.2.46 created 2015
Pathway
ec00998 Biosynthesis of various antibiotics
ec01110 Biosynthesis of secondary metabolites
Orthology
K22113 fumarate---(S)-2,3-diaminopropanoate ligase
Genes
» show all
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
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.46
ExPASy - ENZYME nomenclature database: 6.3.2.46