Literature summary for 1.13.12.6 extracted from

Mitani, Y.; Yasuno, R.; Kihira, K.; Chung, K.; Mitsuda, N.; Kanie, S.; Tomioka, A.; Kaji, H.; Ohmiya, Y.
Host-dependent producibility of recombinant Cypridina noctiluca luciferase with glycosylation defects (2022), Front. Bioeng. Biotechnol., 10, 774786 .

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Application

Application	Comment	Organism
analysis	the thermostable enzyme can be used for various research applications, including in vivo imaging and high throughput reporter assays	Cypridina noctiluca
molecular biology	the thermostable enzyme can be used for various research applications, including in vivo imaging and high throughput reporter assays	Cypridina noctiluca

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant mutant enzyme lacking N-glycosylation motifs is produced using Expi293F cells, silkworms, and tobacco BY-2 cells. The relative activity of the produced Dmt CLucEX is almost the same as that of the wild-type CLucEX, whereas recombinant CLuc deficient in N-glycosylation binding sites (Dmt CLucCO) is approximately 20% of that of wild-type CLucCO. In the case of the silkworm system, the relative activity of mutant CLuc purified using only anti-FLAG affinity gel is 25% of that of wild-type CLucSW. However, further purification reveals that approximately 75% of the FLAG purified recombinant protein is aggregated and its enzyme activity is lost. In the BY-2 cells, attempt to express Dmt CLucBY result in no recombinant protein production despite the use of 4 independent transgenic callus clones. The productivity of CLuc mutated in the N-glycosylation sites differs depending on the expression host	Cypridina noctiluca

Cloned (Comment)

Organism

recombinant mutant enzyme lacking N-glycosylation motifs is produced using Expi293F cells, silkworms, and tobacco BY-2 cells. The relative activity of the produced Dmt CLucEX is almost the same as that of the wild-type CLucEX, whereas recombinant CLuc deficient in N-glycosylation binding sites (Dmt CLucCO) is approximately 20% of that of wild-type CLucCO. In the case of the silkworm system, the relative activity of mutant CLuc purified using only anti-FLAG affinity gel is 25% of that of wild-type CLucSW. However, further purification reveals that approximately 75% of the FLAG purified recombinant protein is aggregated and its enzyme activity is lost. In the BY-2 cells, attempt to express Dmt CLucBY result in no recombinant protein production despite the use of 4 independent transgenic callus clones. The productivity of CLuc mutated in the N-glycosylation sites differs depending on the expression host

Cypridina noctiluca

Protein Variants

Protein Variants	Comment	Organism
T184A/N404D	both N-glycosylation sites are mutated and lost	Cypridina noctiluca

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Cypridina luciferin + O2	Cypridina noctiluca	-	oxidized Cypridina luciferin + CO2 + hv	-	?

Organism

Organism	UniProt	Comment	Textmining
Cypridina noctiluca	Q75R40	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	N-glycosylation sites: T184 and N404	Cypridina noctiluca

Purification (Commentary)

Purification (Comment)	Organism
-	Cypridina noctiluca

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Cypridina luciferin + O2	-	Cypridina noctiluca	oxidized Cypridina luciferin + CO2 + hv	-	?

Synonyms

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