| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor |
| ID: | 1.14.11.4 | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Description: | Procollagen-lysine 5-dioxygenase. | ||||||||||||||
| Alternative Name: |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase. Lysyl hydroxylase. Lysine,2-oxoglutarate 5-dioxygenase. Lysine hydroxylase. | ||||||||||||||
| Prosite: | PDOC51471; PDOC01028; | ||||||||||||||
| PDB: |
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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 1.14.11.4 |
| BRENDA Enzyme Link: | BRENDA 1.14.11.4 |
| KEGG Enzyme Link: | KEGG1.14.11.4 |
| BioCyc Enzyme Link: | BioCyc 1.14.11.4 |
| ExPASy Enzyme Link: | ExPASy1.14.11.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.11.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.4 |
| IntEnz Enzyme Link: | IntEnz 1.14.11.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.11.4 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:16569 | 2-oxoglutarate + L-lysyl-[procollagen] + O2 = (5R)-5-hydroxy-L-lysyl-[procollagen] + CO2 + succinate |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein. | Turpeenniemi-Hujanen TM, Puistola U, Kivirikko KI | 1980 Aug 1 | 6779811 |
| Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects. | Puistola U, Turpeenniemi-Hujanen TM, Myllylä R, Kivirikko KI | 1980 Jan 11 | 6766066 |
| Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen. | Hausmann E | 1967 Apr 11 | 6033801 |
| Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase. | Rhoads RE, Udenfriend S | 1968 Aug | 5244754 |
| Mimivirus collagen is modified by bifunctional lysyl hydroxylase and glycosyltransferase enzyme. | Luther KB, Hülsmeier AJ, Schegg B, Deuber SA, Raoult D, Hennet T | 2011 Dec 23 | 22045808 |
| The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion. | Norman KR, Moerman DG | 2000 Nov 15 | 11071784 |