Cloned (Comment) | Organism |
---|---|
expression of wild-type and randomly generated mutants in Escherichia coli strain BL21 | Photorhabdus luminescens |
Protein Variants | Comment | Organism |
---|---|---|
D232G | random mutagenesis, 63% of wild-type luminescence activity | Photorhabdus luminescens |
E175G | random mutagenesis, the single point mutation leads to increased decay rate of the enzyme, 0.9% of wild-type luminescence activity | Photorhabdus luminescens |
E175G/N199D | random mutagenesis, 0.1% of wild-type luminescence activity | Photorhabdus luminescens |
K202R | random mutagenesis, 95% of wild-type luminescence activity | Photorhabdus luminescens |
M190T | random mutagenesis, 29% of wild-type luminescence activity | Photorhabdus luminescens |
T198S | random mutagenesis, 84% of wild-type luminescence activity | Photorhabdus luminescens |
General Stability | Organism |
---|---|
the wild-type enzyme belongs to the group of luciferases with slow decay, mutant E175G is turned into a luciferase with fast decay, the decay rate of the enzyme is determined by residue Glu175 | Photorhabdus luminescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Photorhabdus luminescens | the decay rate of the enzyme is determined by residue Glu175 of the central region of the LuxA subunit, distinction between slow and fast decay luciferases is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase-flavin-oxygen intermediate | ? | - |
? | |
RCHO + FMNH2 + O2 | Photorhabdus luminescens | long-chain aldehydes | RCOOH + FMN + H2O + hn | long-chain fatty acids, bioluminescence reaction | ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Photorhabdus luminescens | - |
i.e. Photorhabdus luminescens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the decay rate of the enzyme is determined by residue Glu175 of the central region of the LuxA subunit, distinction between slow and fast decay luciferases is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase-flavin-oxygen intermediate | Photorhabdus luminescens | ? | - |
? | |
additional information | substrate specificity and quantum yield of mutant E175G as a function of aldehyde chain length | Photorhabdus luminescens | ? | - |
? | |
RCHO + FMNH2 + O2 | long-chain aldehydes | Photorhabdus luminescens | RCOOH + FMN + H2O + hn | long-chain fatty acids, bioluminescence reaction | ir |
Synonyms | Comment | Organism |
---|---|---|
bacterial luciferase | - |
Photorhabdus luminescens |
LuxAB | - |
Photorhabdus luminescens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
23 | - |
assay at | Photorhabdus luminescens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Photorhabdus luminescens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMNH2 | - |
Photorhabdus luminescens |