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Literature summary extracted from

  • Hosseinkhani, S.; Szittner, R.; Meighen, E.A.
    Random mutagenesis of bacterial luciferase: critical role of Glu175 in the control of luminescence decay (2005), Biochem. J., 385, 575-580.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.3 expression of wild-type and randomly generated mutants in Escherichia coli strain BL21 Photorhabdus luminescens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.3 D232G random mutagenesis, 63% of wild-type luminescence activity Photorhabdus luminescens
1.14.14.3 E175G random mutagenesis, the single point mutation leads to increased decay rate of the enzyme, 0.9% of wild-type luminescence activity Photorhabdus luminescens
1.14.14.3 E175G/N199D random mutagenesis, 0.1% of wild-type luminescence activity Photorhabdus luminescens
1.14.14.3 K202R random mutagenesis, 95% of wild-type luminescence activity Photorhabdus luminescens
1.14.14.3 M190T random mutagenesis, 29% of wild-type luminescence activity Photorhabdus luminescens
1.14.14.3 T198S random mutagenesis, 84% of wild-type luminescence activity Photorhabdus luminescens

General Stability

EC Number General Stability Organism
1.14.14.3 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.3 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 ?
-
 ?
1.14.14.3 RCHO + FMNH2 + O2 Photorhabdus luminescens long-chain aldehydes RCOOH + FMN + H2O + hn long-chain fatty acids, bioluminescence reaction ir

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.3 Photorhabdus luminescens
-
 i.e. Photorhabdus luminescens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.3 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 ?
-
 ?
1.14.14.3 additional information substrate specificity and quantum yield of mutant E175G as a function of aldehyde chain length Photorhabdus luminescens ?
-
 ?
1.14.14.3 RCHO + FMNH2 + O2 long-chain aldehydes Photorhabdus luminescens RCOOH + FMN + H2O + hn long-chain fatty acids, bioluminescence reaction ir

Synonyms

EC Number Synonyms Comment Organism
1.14.14.3 bacterial luciferase
-
 Photorhabdus luminescens
1.14.14.3 LuxAB
-
 Photorhabdus luminescens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.3 23
-
 assay at Photorhabdus luminescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.3 7
-
 assay at Photorhabdus luminescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.3 FMNH2
-
 Photorhabdus luminescens