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Literature summary for 1.13.12.6 extracted from

  • Yasuno, R.; Mitani, Y.; Ohmiya, Y.
    Effects of N-glycosylation deletions on Cypridina luciferase activity (2018), Photochem. Photobiol., 94, 338-342 .
    View publication on PubMed
Search for more literature for 1.13.12.6

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in COS-1 cells and in Pichia pastoris strain GS115 Cypridina noctiluca

Protein Variants

Protein Variants Comment Organism
additional information wild-type and mutant enzymes show similar secretion efficiencies, and thermostabilities at 25-37°C, overview Cypridina noctiluca
N182D site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant enzyme behaves similar compared to the wild-type Cypridina noctiluca
N182D/N404D site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type Cypridina noctiluca
N182D/S406A site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type Cypridina noctiluca
N404D site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant enzyme behaves similar to the wild-type Cypridina noctiluca
S406A site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows increased protein accumulation compared to the wild-type Cypridina noctiluca
T184A site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows increased protein accumulation compared to the wild-type Cypridina noctiluca
T184A/N404D site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over 2.5fold increased protein accumulation compared to the wild-type Cypridina noctiluca
T184A/S406A site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type Cypridina noctiluca

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Cypridina noctiluca
-
-

Organism

Organism UniProt Comment Textmining
Cypridina noctiluca Q75R40
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme has two N-glycosylation sites with the consensus sequence for N-glycosylation (Asn-X-Ser/Thr). The producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. N-glycosylation modifications and the proper amino acid sequence of the N-glycan binding sites of Cluc are required for the complete protein folding to form a stable catalytic center, for the proper conformation of substrate-protein interaction residues, or for both. Defects in the glycosylation modification are not related to secretion process and stability of the protein Cypridina noctiluca

Subunits

Subunits Comment Organism
? x * 60000, mature enzyme Cluc, SDS-PAGE Cypridina noctiluca

Synonyms

Synonyms Comment Organism
CLuc
-
 Cypridina noctiluca
Cypridina luciferase
-
 Cypridina noctiluca

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Cypridina noctiluca

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Cypridina noctiluca

General Information

General Information Comment Organism
malfunction Producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. Defects in the glycosylation modification are not related to secretion process and stability of the protein Cypridina noctiluca