Information on EC 1.13.12.8 - Watasenia-luciferin 2-monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.13.12.8
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RECOMMENDED NAME
GeneOntology No.
Watasenia-luciferin 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Watasenia luciferin + O2 = oxidized Watasenia luciferin + CO2 + hnu
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
Watasenia-luciferin:oxygen 2-oxidoreductase (decarboxylating)
The enzyme from the luminous squid Watasenia may be assayed by measurement of light emission.
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
evolution
physiological function
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the organism produces flashes of blue light via a series of complicated luciferin-luciferase reactions involving ATP, Mg2+, and molecular oxygen. The enzyme catalyzes the two key steps. They are the addition of molecular oxygen to luciferin and the formation of light emitter. The oxygenation reaction occurs with a single electron-transfer (SET) mechanism, and the light emitter is produced via the mechanism of gradually reversible charge-transfer-induced luminescence (GRCTIL). Biolumiscence key steps are oxygenation of luciferin and thermolysis of the peroxide intermediate to produce light emitter
additional information
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protein microcrystals in the arm photophores catalyse the bioluminescent reaction using ATP and the substrate coelenterazine disulfate. The crystals contain a major 63 kDa protein and a minor 81 kDa protein, in a mass ratio of about 8 to 1. Three homologous proteins comprise the luminescent arm tip microcrystals, i.e. proteins wsluc1-3, wsluc1-3 form a complex that crystallises inside the squid photophores. Analysis of the proteins from the protein crystal extraction identified by MALDI TOF/TOF mass spectrometry analysis, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coelenterazine disulfate + O2 + ATP
? + CO2 + hv + AMP
show the reaction diagram
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strictly specific substrate
light emitter is the excited state of the anion form of coelerenterazine disulfate, quantum yield is calculated at 0.36. the reaction mechanism does not involve formation of a adenyl luciferin intermediate
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?
coelenterazine disulfate + O2 + ATP-gamma-S
? + CO2 + hv
show the reaction diagram
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strictly specific substrate
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?
long chain aldehyde + FMNH2 + O2
corresponding fatty acid + FMN + H2O + hv
show the reaction diagram
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-
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?
luciferin + O2
oxidized luciferin + CO2 + hv
show the reaction diagram
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-
-
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?
Watasenia luciferin + O2
oxidized Watasenia luciferin + CO2 + h?
show the reaction diagram
Watasenia luciferin + O2
oxidized Watasenia luciferin + CO2 + hv
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Watasenia luciferin + O2
oxidized Watasenia luciferin + CO2 + h?
show the reaction diagram
Watasenia luciferin + O2
oxidized Watasenia luciferin + CO2 + hv
show the reaction diagram
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bioluminescence
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required for activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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kinetics and thermodynamics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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dermal photogenic organs, distributed along the ventral aspects of the head, matle, funnel, arms and eyes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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insoluble
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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protein crystals show two bands of approximately 59 and 81 kDa in a ratio of 4:1 or 5:1
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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15 min, 90% loss of activity
additional information
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enzyme is sensitive to freezing
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40°C, supernatant with high concentrations of enzyme, several years, little loss of activity
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-40°C, tissue homogenate, 24 h, 35% loss of activity
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-80°C, tissue homogenate, several days, complete loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose chromatography
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partial purification as particulate, in presence of high concentration of sucrose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3)(pLysS) cells
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expressed in Mycobacterium tuberculosis strain H37Ra
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expressed in Streptomyces lividans starin TK 24
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three proteins termed wsluc1 (encoded by transcript 82699_c0_seq1), wsluc2 (81000_c2_seq2) and wsluc3 (83251_c0_seq1), sequence comparisons and phylogenetic analysis, transcriptome analysis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E175G
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mutation changes the enzymatic decay rate by inducing a substantial tertiary structural change, without a large effect on secondary structural elements