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Information on EC 1.14.14.3 - bacterial luciferase

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IUBMB Comments
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, dinoflagellate luciferase.
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This record set is specific for:
UNIPROT: P09142
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
luciferase, bacterial luciferase, luxab, luxcdabe, vibrio harveyi luciferase, vibrio fischeri luciferase, aldehyde monooxygenase, gluc luciferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde monooxygenase
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alkanal monooxygenase (FMN)
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bacterial luciferase
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luciferase
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Vibrio fischeri luciferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
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, dinoflagellate luciferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-00-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isolated dimeric LuxF binds four molecules of the derivatized flavin, 6-(3'-(R)-myristyl)-FMN. LuxF binds myrFMN tightly with a dissociation constant of 80 nM
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUXF_PHOLE
228
0
26239
Swiss-Prot
Mitochondrion (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme, to 1.85 A resolution. Apo-LuxF possesses four preorganized binding sites for 6-(3'-(R)-myristyl)-FMN
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bergner, T.; Tabib, C.R.; Winkler, A.; Stipsits, S.; Kayer, H.; Lee, J.; Malthouse, J.P.; Mayhew, S.; Mueller, F.; Gruber, K.; Macheroux, P.
Structural and biochemical properties of LuxF from Photobacterium leiognathi
Biochim. Biophys. Acta
1854
1466-1475
2015
Photobacterium leiognathi (P09142), Photobacterium leiognathi, Photobacterium leiognathi S1 (P09142)
Manually annotated by BRENDA team