| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.13.59 |
|---|---|
| Description: | L-lysine N(6)-monooxygenase (NADPH). |
| Alternative Name: |
Lysine N(6)-hydroxylase. |
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 1.14.13.59 |
| BRENDA Enzyme Link: | BRENDA 1.14.13.59 |
| KEGG Enzyme Link: | KEGG1.14.13.59 |
| BioCyc Enzyme Link: | BioCyc 1.14.13.59 |
| ExPASy Enzyme Link: | ExPASy1.14.13.59 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.13.59 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.59 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.59 |
| IntEnz Enzyme Link: | IntEnz 1.14.13.59 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.13.59 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:23228 | L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+) |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[NH2;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:9]-[NH;+0:10]-[OH;+0:11].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:12] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222. | Macheroux P, Plattner HJ, Romaguera A, Diekmann H | 1993 May 1 | 8504838 |
| Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase. | Thariath AM, Fatum KL, Valvano MA, Viswanatha T | 1993 Nov 10 | 8218389 |
| Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. | de Lorenzo V, Bindereif A, Paw BH, Neilands JB | 1986 Feb | 2935523 |
| Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222. | Plattner HJ, Pfefferle P, Romaguera A, Waschütza S, Diekmann H | 1989 | 2518519 |
| Studies on lysine:N6-hydroxylation by cell-free systems of Aerobacter aerogenes 62-1. | Goh CJ, Szczepan EW, Menhart N, Viswanatha T | 1989 Mar 24 | 2493814 |
| Recombinant lysine:N(6)-hydroxylase: effect of cysteine-->alanine replacements on structural integrity and catalytic competence. | Dick S, Siemann S, Frey HE, Lepock JR, Viswanatha T | 2002 Feb 11 | 11904218 |