ENZYME entry: EC 1.14.14.3
Accepted Name |
bacterial luciferase.
|
Alternative Name(s) |
aldehyde monooxygenase. |
alkanal monooxygenase (FMN-linked). |
Reaction catalysed |
a long-chain fatty aldehyde + FMNH2 + O2 <=> a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu |
Comment(s) |
- The reaction sequence starts with the incorporation of a molecule of
oxygen into reduced FMN bound to the enzyme, forming luciferase
peroxyflavin.
- The peroxyflavin interacts with an aliphatic long-chain aldehyde,
producing a highly fluorescent species believed to be luciferase
hydroxyflavin.
- The enzyme is highly specific for reduced FMN and for long-chain
aliphatic aldehydes with eight carbons or more.
- The highest efficiency is achieved with tetradecanal. cf.
EC 1.13.12.18.
|
Cross-references |
BRENDA | 1.14.14.3 |
EC2PDB | 1.14.14.3 |
ExplorEnz | 1.14.14.3 |
PRIAM enzyme-specific profiles | 1.14.14.3 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.14.3 |
IUBMB Enzyme Nomenclature | 1.14.14.3 |
IntEnz | 1.14.14.3 |
MEDLINE | Find literature relating to 1.14.14.3 |
MetaCyc | 1.14.14.3 |
Rhea expert-curated reactions | 1.14.14.3 |
UniProtKB/Swiss-Prot |
P09140, LUXA1_PHOLE; | P19839, LUXA1_PHOLU; | P29238, LUXA2_PHOLE; |
P23146, LUXA2_PHOLU; | P19907, LUXA_ALIFS; | P18299, LUXA_KRYAS; |
Q7N575, LUXA_PHOLL; | P24113, LUXA_PHOPO; | P24114, LUXA_VIBCL; |
P07740, LUXA_VIBHA; | P09141, LUXB1_PHOLE; | P19840, LUXB1_PHOLU; |
P29239, LUXB2_PHOLE; | P23147, LUXB2_PHOLU; | P19908, LUXB_ALIFS; |
P18300, LUXB_KRYAS; | Q7N574, LUXB_PHOLL; | P12744, LUXB_PHOPO; |
P07739, LUXB_VIBHA; |
|
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