| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.2 Acid-D-amino-acid ligases (peptide synthases) |
| ID: | 6.3.2.47 |
|---|---|
| Description: | Dapdiamide synthase. |
| Alternative Name: |
Dapdiamide A synthase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 6.3.2.47 |
| BRENDA Enzyme Link: | BRENDA 6.3.2.47 |
| KEGG Enzyme Link: | KEGG6.3.2.47 |
| BioCyc Enzyme Link: | BioCyc 6.3.2.47 |
| ExPASy Enzyme Link: | ExPASy6.3.2.47 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.2.47 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.2.47 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.2.47 |
| IntEnz Enzyme Link: | IntEnz 6.3.2.47 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.2.47 |
| RHEA:44344 | ATP + L-valine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide A + H(+) + phosphate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. | Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM Jr, Kelleher NL, Walsh CT | 2010 Nov 10 | 20945916 |
| The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. | Hollenhorst MA, Clardy J, Walsh CT | 2009 Nov 3 | 19807062 |
| RHEA:44348 | ATP + L-isoleucine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide B + H(+) + phosphate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. | Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM Jr, Kelleher NL, Walsh CT | 2010 Nov 10 | 20945916 |
| The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. | Hollenhorst MA, Clardy J, Walsh CT | 2009 Nov 3 | 19807062 |
| RHEA:44352 | ATP + L-leucine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide C + H(+) + phosphate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. | Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM Jr, Kelleher NL, Walsh CT | 2010 Nov 10 | 20945916 |
| The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. | Hollenhorst MA, Clardy J, Walsh CT | 2009 Nov 3 | 19807062 |
| RHEA:45080 | 3-[[[(2R,3R)-3-carboxyoxiran-2-yl]carbonyl]amino]-L-alanine + ATP + L-valine = ADP + dapdiamide E + H(+) + phosphate |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:12]-[OH;+0:11].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. | Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM Jr, Kelleher NL, Walsh CT | 2010 Nov 10 | 20945916 |
| The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. | Hollenhorst MA, Clardy J, Walsh CT | 2009 Nov 3 | 19807062 |