1.13.12.18: dinoflagellate luciferase
This is an abbreviated version!
For detailed information about dinoflagellate luciferase, go to the full flat file.
Word Map on EC 1.13.12.18
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1.13.12.18
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bioluminescence
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emit
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lingulodinium
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gonyaulax
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luminescence
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tetrapyrrole
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polyedrum
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luciferases
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alexandrium
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circadian
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clap
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whitting
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fundyense
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spinifera
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pyrocystis
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open-chain
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naked
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flash
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intramolecularly
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ph-activity
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lunula
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interspecific
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light-emitting
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catenella
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genus-specific
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biotechnology
- 1.13.12.18
-
bioluminescence
-
emit
-
lingulodinium
- gonyaulax
-
luminescence
- tetrapyrrole
- polyedrum
- luciferases
- alexandrium
-
circadian
-
clap
-
whitting
- fundyense
- spinifera
-
pyrocystis
-
open-chain
-
naked
- flash
-
intramolecularly
-
ph-activity
- lunula
-
interspecific
-
light-emitting
- catenella
-
genus-specific
- biotechnology
Reaction
Synonyms
D2-LCF, D3-LCF, LCF, luciferase
ECTree
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pH Optimum
pH Optimum on EC 1.13.12.18 - dinoflagellate luciferase
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6.3
additional information
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the optimum pH of Lingulodinium polyedrum luciferase and for each of its domains is approximately 6.0
6
constant pH accelerated molecular dynamics (CpHaMD) is applied to investigate the conformational changes associated with the activation of the enzyme (LCF) upon acidification. The protonation of several residues, including the previously identifies intramolecularly conserved histidines and the H1064/H1065 dyad, correlates with a large scale conformational change in which the N-terminal domain reorganizes to allow the substrate access to the active site
the oxidation of luciferin by Dinoflagellates luciferase only takes place at low pH. Computational tools are used to predict the open structure of the luciferase in Lingulodinium polyedra and to decipher the nature of the opening mechanism. Through accelerated molecular dynamics simulations, it is demonstrated that the closed-open conformational change likely takes place via a tilt of the pH-regulatory helix-loop-helix domain. It is proposed that the molecular basis for the transition is electrostatic repulsion between histidine-cation pairs, which destabilizes the closed conformation at low pH
additional information
-
the oxidation of luciferin by Dinoflagellates luciferase only takes place at low pH. Computational tools are used to predict the open structure of the luciferase in Lingulodinium polyedra and to decipher the nature of the opening mechanism. Through accelerated molecular dynamics simulations, it is demonstrated that the closed-open conformational change likely takes place via a tilt of the pH-regulatory helix-loop-helix domain. It is proposed that the molecular basis for the transition is electrostatic repulsion between histidine-cation pairs, which destabilizes the closed conformation at low pH