1.13.12.6: Cypridina-luciferin 2-monooxygenase
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For detailed information about Cypridina-luciferin 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.6
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1.13.12.6
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bioluminescence
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luminescence
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hilgendorfii
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luciferases
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ostracod
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firefly
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analysis
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gaussia
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diagnostics
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molecular biology
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biotechnology
- 1.13.12.6
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bioluminescence
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luminescence
- hilgendorfii
- luciferases
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ostracod
- firefly
- analysis
- gaussia
- diagnostics
- molecular biology
- biotechnology
Reaction
Synonyms
Apogon luciferase, Apogon luciferase 1, CLase, CLuc, Cypridina luciferase, Cypridina luciferin 2-monooxygenase, Cypridina noctiluca luciferase, Cypridina-type luciferase, Fbp, FBP-IgG, luciferase (Cypridina luciferin), PGE2-luciferase, Vargula luciferase
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Posttranslational Modification
Posttranslational Modification on EC 1.13.12.6 - Cypridina-luciferin 2-monooxygenase
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glycoprotein
glycosylation pattern analysis using LCMS/MS. In the recombinnat enzyme, two potential N-glycosylation sites are modified with plant-type oligosaccharide chains. Partial deglycosylation (trimming) of recombinant Cluc by beta-N-acetylhexosaminidase, HexNAc residues at the non-reducing termini of glycopeptides (Pronase E-digested) are completely eliminated at both glycosylation sites after beta-N-acetylhexosaminidase treatment (at Asn182 and Asn404). The glycan compositions after treatment displays trimannosyl cores (Hex3HexNAc2)+/-Fuc+/-Xyl. Specifically, because the trimannosyl core is fully occupied by Fuc and Xyl on Asn404, only a single signal corresponding to the trimannosyl core +Fuc +Xyl remains after treatment. This glycan-trimmed recombinant protein still exhibits nearly the same level of activity as the unmodified glycoprotein
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