| EC Tree |
| 1. Oxidoreductases |
| 1.5 Acting on the CH-NH group of donors |
| 1.5.99 With unknown physiological acceptors |
| ID: | 1.5.99.13 |
|---|---|
| Description: | D-proline dehydrogenase. |
| Alternative Name: |
D-pro DH. D-pro dehydrogenase. |
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 1.5.99.13 |
| BRENDA Enzyme Link: | BRENDA 1.5.99.13 |
| KEGG Enzyme Link: | KEGG1.5.99.13 |
| BioCyc Enzyme Link: | BioCyc 1.5.99.13 |
| ExPASy Enzyme Link: | ExPASy1.5.99.13 |
| EC2PDB Enzyme Link: | EC2PDB 1.5.99.13 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.5.99.13 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.5.99.13 |
| IntEnz Enzyme Link: | IntEnz 1.5.99.13 |
| MEDLINE Enzyme Link: | MEDLINE 1.5.99.13 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:27306 | A + D-proline = 1-pyrroline-2-carboxylate + AH2 |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH;+0:4]-[*:5]>>[*:1]-[C;H0;+0:2](-[*:3])=[N;H0;+0:4]-[*:5] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. | Tani Y, Tanaka K, Yabutani T, Mishima Y, Sakuraba H, Ohshima T, Motonaka J | 2008 Jul 7 | 18558115 |
| Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. | Satomura T, Kawakami R, Sakuraba H, Ohshima T | 2002 Apr 12 | 11823469 |