EC number:1.14.14.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.14.3 |
|---|---|
| Description: | Bacterial luciferase. |
| Alternative Name: |
Alkanal monooxygenase (FMN-linked). Aldehyde monooxygenase. |
| Prosite: | PDOC00397; |
| PDB: |
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| Cath: | 3.20.20.30; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.3 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.3 |
| KEGG Enzyme Link: | KEGG1.14.14.3 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.3 |
| ExPASy Enzyme Link: | ExPASy1.14.14.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.3 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.3 |
EC number:1.14.14.3
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:17181 | a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu |
| RULE(radius=1) | [*:1]-[CH;+0:2]=[*:3].[*:4]-[N;H0;+0:5]1-[*:6]:[*:7]-[NH;+0:8]-[c;H0;+0:9](:[*:10]):[c;H0;+0:11]-1:[nH;+0:12]:[*:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:14].[*:4]-[n;H0;+0:5]1:[*:6]:[*:7]:[n;H0;+0:8]:[c;H0;+0:9](:[*:10])-[c;H0;+0:11]:1:[n;H0;+0:12]:[*:13].[OH2;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Bacterial luciferase: FMNH2-aldehyde oxidase. | Hastings JW, Presswood RP | 1978 | 309549 |
| Activity coupling and complex formation between bacterial luciferase and flavin reductases. | Tu SC | 2008 Feb | 18264585 |
| Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction. | Kurfürst M, Ghisla S, Hastings JW | 1984 May | 16593462 |
| Probing the functionalities of alphaGlu328 and alphaAla74 of Vibrio harveyi luciferase by site-directed mutagenesis and chemical rescue. | Li CH, Tu SC | 2005 Oct 25 | 16229475 |
| Identity of the emitter in the bacterial luciferase luminescence reaction: binding and fluorescence quantum yield studies of 5-decyl-4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate as a model. | Lei B, Ding Q, Tu SC | 2004 Dec 21 | 15595854 |
| Changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform in Vibrio harveyi luciferase. | Lin LY, Szittner R, Friedman R, Meighen EA | 2004 Mar 23 | 15023068 |
| Nucleotide sequence, expression, and properties of luciferase coded by lux genes from a terrestrial bacterium. | Szittner R, Meighen E | 1990 Sep 25 | 2204626 |
| Structure and properties of luciferase from Photobacterium phosphoreum. | Ferri SR, Soly RR, Szittner RB, Meighen EA | 1991 Apr 15 | 2018544 |
| Cloning and nucleotide sequences of lux genes and characterization of luciferase of Xenorhabdus luminescens from a human wound. | Xi L, Cho KW, Tu SC | 1991 Feb | 1995589 |
| The lux genes of the luminous bacterial symbiont, Photobacterium leiognathi, of the ponyfish. Nucleotide sequence, difference in gene organization, and high expression in mutant Escherichia coli. | Lee CY, Szittner RB, Meighen EA | 1991 Oct 1 | 1915359 |