Biosynthesis of coelenterazine in the deep-sea copepod, Metridia pacifica

Oba, Yuichi; Kato, Shin‐ichi; Ojika, Makoto; Inouye, Satoshi

doi:10.1016/j.bbrc.2009.10.028

Cited by 54 publications

(54 citation statements)

References 23 publications

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“…In the luminous ostracods Cypridina (presently Vargula ) hilgendorfii and Cypridina noctiluca , we concluded that Cypridina luciferin is biosynthesized from the natural amino acids of ʟ-tryptophan, ʟ-arginine, and ʟ-isoleucine [9]–[11], [13]. Further, we demonstrated that coelenterazine is biosynthesized from two ʟ-tyrosines and ʟ-phenylalanine in the deep-sea luminous copepod Metridia pacifica [12]. Thus, similar to the method using the radioisotope-labeled compounds, the method of mass spectral analysis accompanied by the incorporation of stable isotope-labeled compounds is useful for investigating the biosynthetic process.…”

Section: Introductionmentioning

confidence: 92%

“…Recently, we have been studying the biosyntheses of Cypridina luciferin and coelenterazine in living specimens by feeding experiments using stable isotope-labeled compounds. The incorporation of stable isotopes into the luciferin was determined by mass spectrometry [9]–[12]. In the luminous ostracods Cypridina (presently Vargula ) hilgendorfii and Cypridina noctiluca , we concluded that Cypridina luciferin is biosynthesized from the natural amino acids of ʟ-tryptophan, ʟ-arginine, and ʟ-isoleucine [9]–[11], [13].…”

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of ʟ-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis

et al. 2013

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BackgroundBioluminescence in fireflies and click beetles is produced by a luciferase-luciferin reaction. The luminescence property and protein structure of firefly luciferase have been investigated, and its cDNA has been used for various assay systems. The chemical structure of firefly luciferin was identified as the ᴅ-form in 1963 and studies on the biosynthesis of firefly luciferin began early in the 1970’s. Incorporation experiments using 14C-labeled compounds were performed, and cysteine and benzoquinone/hydroquinone were proposed to be biosynthetic component for firefly luciferin. However, there have been no clear conclusions regarding the biosynthetic components of firefly luciferin over 30 years.Methodology/Principal FindingsIncorporation studies were performed by injecting stable isotope-labeled compounds, including ʟ-[U-13C3]-cysteine, ʟ-[1-13C]-cysteine, ʟ-[3-13C]-cysteine, 1,4-[D6]-hydroquinone, and p-[2,3,5,6-D]-benzoquinone, into the adult lantern of the living Japanese firefly Luciola lateralis. After extracting firefly luciferin from the lantern, the incorporation of stable isotope-labeled compounds into firefly luciferin was identified by LC/ESI-TOF-MS. The positions of the stable isotope atoms in firefly luciferin were determined by the mass fragmentation of firefly luciferin.ConclusionsWe demonstrated for the first time that ᴅ- and ʟ-firefly luciferins are biosynthesized in the lantern of the adult firefly from two ʟ-cysteine molecules with p-benzoquinone/1,4-hydroquinone, accompanied by the decarboxylation of ʟ-cysteine.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of ʟ-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis

et al. 2013

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“…First, feeding experiments indicate the compound is made from L-Tyr and L-Phe. 475 Second, and more intriguing, expression in E. coli of a mutant of the green fluorescent protein from Aequorea victoria in which the conserved sequence FSYG leading to the GFP chromophore was replaced with FYYG resulted in the production of coelenterazine. 476 At present, no details are available regarding this remarkable observation, but it suggests that coelenterazine can be made from a ribosomally synthesized protein.…”

Section: Pqq Pantocin and Thyroid Hormonesmentioning

confidence: 99%

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature

et al. 2013

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“…Despite these hindrances, the substrate advantage of Lux system is unique and irreplaceable as the biosynthesis pathways for both coelenterazine and d -luciferin are unclear and numerous enzymes will be involved even if they are resolved someday [89,90]. In 2003, a mechanism study about bacterial luciferase shows that energy transfer between LuxAB and YFP is possible [91], and, in 2014, Cui et al reported the first LuxAB based BRET system and it is proven to be useful and relatively reliable [28].…”

Section: Developed Bret Systems and Their Applicationsmentioning

confidence: 99%

In Vivo Analysis of Protein–Protein Interactions with Bioluminescence Resonance Energy Transfer (BRET): Progress and Prospects

Sun

Yang

Wang

et al. 2016

IJMS

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Proteins are the elementary machinery of life, and their functions are carried out mostly by molecular interactions. Among those interactions, protein–protein interactions (PPIs) are the most important as they participate in or mediate all essential biological processes. However, many common methods for PPI investigations are slightly unreliable and suffer from various limitations, especially in the studies of dynamic PPIs. To solve this problem, a method called Bioluminescence Resonance Energy Transfer (BRET) was developed about seventeen years ago. Since then, BRET has evolved into a whole class of methods that can be used to survey virtually any kinds of PPIs. Compared to many traditional methods, BRET is highly sensitive, reliable, easy to perform, and relatively inexpensive. However, most importantly, it can be done in vivo and allows the real-time monitoring of dynamic PPIs with the easily detectable light signal, which is extremely valuable for the PPI functional research. This review will take a comprehensive look at this powerful technique, including its principles, comparisons with other methods, experimental approaches, classifications, applications, early developments, recent progress, and prospects.

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Biosynthesis of coelenterazine in the deep-sea copepod, Metridia pacifica

Cited by 54 publications

References 23 publications

Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of ʟ-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis

Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of ʟ-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature

In Vivo Analysis of Protein–Protein Interactions with Bioluminescence Resonance Energy Transfer (BRET): Progress and Prospects

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