KEGG ENZYME: 6.3.2.47

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)

R10941 R10942 R10943 R10944

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

SPE:

Spro_0344

SPLY:

Q5A_016905(purD_2)

PVA:	Pvag_pPag20162 Pvag_pPag20163

PAGC:

BEE12_22710

XGR:	QL128_02000(ddaF)

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

[ag:ADN39488]

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

[ag:ADN39488]

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

DBGET integrated database retrieval system