Bioluminescence of ()-Cypridina Luciferin with Luciferase.

Cypridina luciferin (CypL) is a marine natural product that functions as the luminous substrate for the enzyme luciferase (CypLase). CypL has two enantiomers, ()- and ()-CypL, due to its one chiral center at the -butyl moiety. Previous studies reported that ()-CypL or racemic CypL with CypLase produced light, but the luminescence of ()-CypL with CypLase has not been investigated.

An international validation study of the interleukin-2 luciferase leukocyte toxicity test (IL-2 Luc LTT) to evaluate potential immunosuppressive chemicals and its performance after use with the interleukin-2 luciferase assay (IL-2 Luc assay).

We previously reported that the IL-2 Luc LTT can detect immunosuppressive effects of drugs that are attributed to their antimitotic activity. Here, we report an official validation study of the IL-2 Luc LTT. In the Phase I study that evaluated five coded chemicals, the within-laboratory reproducibility of three independent laboratories was 100.

Gene Cloning and Functional Analysis of the Luciferase from Luminous Syllids of the Genus Odontosyllis.

The marine fireworm Odontosyllis spp. produce the bluish-green bioluminescence (BL). Despite years of research, molecular mechanisms of this unique luciferin-luciferase reaction have not been elucidated.

Host-Dependent Producibility of Recombinant Luciferase With Glycosylation Defects.

luciferase (CLuc) is a secreted luminescent protein that reacts with its substrate (Cypridina luciferin) to emit light. CLuc is known to be a thermostable protein and has been used for various research applications, including imaging and high-throughput reporter assays. Previously, we produced a large amount of recombinant CLuc for crystallographic analysis.

An international validation study of the IL-2 Luc assay for evaluating the potential immunotoxic effects of chemicals on T cells and a proposal for reference data for immunotoxic chemicals.

To evaluate the immunotoxic effects of xenobiotics, we have established the Multi-ImmunoTox assay, in which three stable reporter cell lines are used to evaluate the effects of chemicals on the IL-2, IFN-γ, IL-1β and IL-8 promoters. Here, we report the official validation study of the IL-2 luciferase assay (IL-2 Luc assay). In the Phase I study that evaluated five coded chemicals in three sets of experiments, the average within-laboratory reproducibility was 86.

Luciferase gene of a Caribbean fireworm (Syllidae) from Puerto Rico.

The fireworms Odontosyllis spp. are globally distributed and well-known for their characteristic and fascinating mating behavior, with secreted mucus emitting bluish-green light. However, knowledge about the molecules involved in the light emission are still scarce.

Novel application of Macrolampis sp2 firefly luciferase for intracellular pH-biosensing in mammalian cells.

Bioluminescence is widely used in biosensors. Firefly luciferase-based bioluminescent sensors are among the most popular ones. Firefly luciferases are pH-sensitive, displaying a large red shift at acidic pH, a property that has been considered undesirable for most applications.

Novel gene encoding a unique luciferase from the fireworm Odontsyllis undecimdonta.

Luciferases identified or engineered so far emit violet, blue, blue-green, green, yellow, red or near infra-red light. The unique and beautiful bluish-green bioluminescence of fireworms Odontosyllis spp. has attracted particular interest, however, their molecular basis is totally unknown partly due to the difficulty of animal collection.

Effects of N-Glycosylation Deletions on Cypridina Luciferase Activity.

Cypridina luciferase (Cluc), a secreted luminescent protein identified from Cypridina noctiluca, has two N-glycosylation sites. In this study, we evaluated the effects of N-glycosylation on Cluc properties by creating site-directed mutagenic modifications at the consensus sequence for N-glycosylation (Asn-X-Ser/Thr). Eight variants consisting of four single- and double-residue mutants each were characterized.

Identification and molecular characterization of the beta-ketoacyl-[acyl carrier protein] synthase component of the Arabidopsis mitochondrial fatty acid synthase.

Substrate specificity of condensing enzymes is a predominant factor determining the nature of fatty acyl chains synthesized by type II fatty acid synthase (FAS) enzyme complexes composed of discrete enzymes. The gene (mtKAS) encoding the condensing enzyme, beta-ketoacyl-[acyl carrier protein] (ACP) synthase (KAS), constituent of the mitochondrial FAS was cloned from Arabidopsis thaliana, and its product was purified and characterized. The mtKAS cDNA complemented the KAS II defect in the E.

The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana.

In eukaryotes, the biosynthetic pathway for lipoic acid is present in mitochondria. However, it has been hypothesized that, in plants, the biosynthetic pathway is present in plastids in addition to mitochondria. In this study, Arabidopsis thaliana LIP1p cDNA for a plastidial form of lipoic acid synthase has been identified.