| EC Tree |
| 1. Oxidoreductases |
| 1.21 Catalysing the reaction X-H + Y-H = X-Y |
| 1.21.98 With other, known, physiological acceptors |
| ID: | 1.21.98.2 |
|---|---|
| Description: | Dichlorochromopyrrolate 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 1.21.98.2 |
| BRENDA Enzyme Link: | BRENDA 1.21.98.2 |
| KEGG Enzyme Link: | KEGG1.21.98.2 |
| BioCyc Enzyme Link: | BioCyc 1.21.98.2 |
| ExPASy Enzyme Link: | ExPASy1.21.98.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.21.98.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.21.98.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.21.98.2 |
| IntEnz Enzyme Link: | IntEnz 1.21.98.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.21.98.2 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:50920 | 2 2-iminio-3-(indol-3-yl)propanoate + H2O2 = chromopyrrolate + H(+) + 2 H2O + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[NH;+0:3])-[CH2;+0:4]-[c;H0;+0:5](:[*:6]):[*:7].[*:8]:[c;H0;+0:9](:[*:10])-[CH2;+0:11]-[C;H0;+0:12](-[*:13])=[NH;+0:14].[OH;+0:15]-[OH;+0:16]>>[*:8]:[c;H0;+0:9](:[*:10])-[c;H0;+0:11]1:[c;H0;+0:4](-[c;H0;+0:5](:[*:6]):[*:7]):[c;H0;+0:2](-[*:1]):[nH;+0:14]:[c;H0;+0:12]:1-[*:13].[NH3;+0:3].[OH2;+0:15].[OH2;+0:16] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum. | Balibar CJ, Walsh CT | 2006 Dec 26 | 17176066 |
| Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD. | Spolitak T, Ballou DP | 2015 May 1 | 25837855 |
| Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. | Howard-Jones AR, Walsh CT | 2005 Dec 6 | 16313168 |
| RHEA:27393 | 2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + H(+) + 2 H2O + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[NH;+0:3])-[CH2;+0:4]-[c;H0;+0:5](:[*:6]):[*:7].[*:8]:[c;H0;+0:9](:[*:10])-[CH2;+0:11]-[C;H0;+0:12](-[*:13])=[NH;+0:14].[OH;+0:15]-[OH;+0:16]>>[*:8]:[c;H0;+0:9](:[*:10])-[c;H0;+0:11]1:[c;H0;+0:4](-[c;H0;+0:5](:[*:6]):[*:7]):[c;H0;+0:2](-[*:1]):[nH;+0:14]:[c;H0;+0:12]:1-[*:13].[NH3;+0:3].[OH2;+0:15].[OH2;+0:16] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD. | Spolitak T, Ballou DP | 2015 May 1 | 25837855 |
| Enzymatic assembly of the bis-indole core of rebeccamycin. | Nishizawa T, Grüschow S, Jayamaha DH, Nishizawa-Harada C, Sherman DH | 2006 Jan 25 | 16417354 |
| Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. | Howard-Jones AR, Walsh CT | 2005 Dec 6 | 16313168 |