BRENDA - Enzyme Database show
show all sequences of 6.2.1.52

Biosynthesis-inspired deracemizative production of D-luciferin by combining luciferase and thioesterase

Maeda, J.; Kato, D.; Okuda, M.; Takeo, M.; Negoro, S.; Arima, K.; Ito, Y.; Niwa, K.; Biochim. Biophys. Acta 1861, 2112-2118 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Luciola cruciata
Inhibitors
Inhibitors
Commentary
Organism
Structure
DL-alpha-lipoic acid
-
Luciola cruciata
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-firefly luciferin + CoA
Luciola cruciata
-
AMP + diphosphate + L-firefly luciferyl-CoA
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Luciola cruciata
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-firefly luciferin + CoA
-
744417
Luciola cruciata
AMP + diphosphate + L-firefly luciferyl-CoA
-
-
-
r
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Luciola cruciata
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
DL-alpha-lipoic acid
-
Luciola cruciata
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-firefly luciferin + CoA
Luciola cruciata
-
AMP + diphosphate + L-firefly luciferyl-CoA
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-firefly luciferin + CoA
-
744417
Luciola cruciata
AMP + diphosphate + L-firefly luciferyl-CoA
-
-
-
r
Other publictions for EC 6.2.1.52
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744417
Maeda
Biosynthesis-inspired deracem ...
Luciola cruciata
Biochim. Biophys. Acta
1861
2112-2118
2017
-
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1
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1
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1
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4
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1
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1
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1
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1
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1
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-
-
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745978
Prado
Structural evolution of lucif ...
Zophobas atratus
Photochem. Photobiol. Sci.
10
1226-1232
2011
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-
-
-
1
-
-
-
-
-
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1
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4
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1
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1
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1
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1
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745606
Leitao
Firefly luciferase inhibition ...
Photinus pyralis
J. Photochem. Photobiol. B
101
1-8
2010
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-
-
-
-
-
30
-
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1
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1
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1
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30
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1
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1
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745980
Viviani
-
The origin of luciferase acti ...
Zophobas atratus
Photochem. Photobiol. Sci.
9
1111-1119
2010
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-
1
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2
-
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1
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1
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1
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1
1
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2
1
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1
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2
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1
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1
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1
1
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2
1
-
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745128
Marques
Firefly bioluminescence A mec ...
Photinus pyralis
IUBMB Life
61
6-17
2009
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-
-
-
-
-
-
-
-
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-
1
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1
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1
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1
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1
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744868
Kato
New application of firefly lu ...
Aquatica lateralis
FEBS J.
274
3877-3885
2007
-
-
-
-
-
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-
1
-
1
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1
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5
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13
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1
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1
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1
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1
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13
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1
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744214
Nakamura
Firefly luciferase exhibits b ...
Photinus pyralis
Biochem. Biophys. Res. Commun.
331
471-475
2005
-
-
-
-
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-
1
1
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1
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1
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1
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1
1
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1
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744710
Fraga
Identification of luciferyl a ...
Photinus pyralis
ChemBioChem
5
110-115
2004
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1
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1
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1
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1
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