Simple Method of Anaerobic Cultivation, with Removal of Oxygen by a Buffered Glucose Oxidase-Catalase System

Fabián, J.

doi:10.1128/jb.89.3.921-921.1965

Cited by 15 publications

(15 citation statements)

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“…The structural similarity between CBDA synthase and THCA synthase suggests that the CBDA synthase reaction proceeds through a mechanism similar to that of the THCA synthase reaction. Therefore, we evaluated the effect of molecular oxygen on the CBDA synthase reaction using a glucose-glucose oxidase-catalase system, which completely consumes the molecular oxygen in assay solutions [19]. Consequently, the CBDA synthase reaction was completely inhibited by this treatment, confirming that the reaction absolutely depends on molecular oxygen.…”

Section: Heterologous Expression Of Cbda Synthase In Insect Cellmentioning

confidence: 90%

“…To examine the molecular oxygen requirement of CBDA synthase, the substrate and enzyme solutions were pre-incubated with glucose oxidase and catalase in the presence of glucose [19]. The hydrogen peroxide generated after the CBDA synthase reaction was quantified using a horseradish peroxidase with 4-aminoantipyrine as substrate [20].…”

Section: Cbda Synthase Assaymentioning

confidence: 99%

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Cannabidiolic‐acid synthase, the chemotype‐determining enzyme in the fiber‐type Cannabis sativa

et al. 2007

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Cannabidiolic-acid (CBDA) synthase is the enzyme that catalyzes oxidative cyclization of cannabigerolic-acid into CBDA, the dominant cannabinoid constituent of the fiber-type Cannabis sativa. We cloned a novel cDNA encoding CBDA synthase by reverse transcription and polymerase chain reactions with degenerate and gene-specific primers. Biochemical characterization of the recombinant enzyme demonstrated that CBDA synthase is a covalently flavinylated oxidase. The structural and functional properties of CBDA synthase are quite similar to those of tetrahydrocannabinolic-acid (THCA) synthase, which is responsible for the biosynthesis of THCA, the major cannabinoid in drug-type Cannabis plants.

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Section: Heterologous Expression Of Cbda Synthase In Insect Cellmentioning

confidence: 90%

Section: Cbda Synthase Assaymentioning

confidence: 99%

Cannabidiolic‐acid synthase, the chemotype‐determining enzyme in the fiber‐type Cannabis sativa

et al. 2007

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“…Divalent metal ions, which are often used as cofactors for class I and class II terpene cyclases (Baunach et al, 2015), also exhibited little effect on enzyme activity (Supplemental Table S1). In contrast, the reaction absolutely required molecular oxygen, because an oxygen-removing treatment using Glc oxidase and catalase in the presence of Glc (Fabian, 1965) completely abolished DCA synthase activity (Table I). Molecular oxygen would participate as the final electron acceptor in the reaction, because hydrogen peroxide, almost in equal quantities to those of DCA, was detected in the reaction mixture with a molar ratio of 1.07 (hydrogen peroxide) versus 1 (DCA).…”

Section: Biochemical Properties Of the Dca Synthase Reactionmentioning

confidence: 99%

Identification and Characterization of Daurichromenic Acid Synthase Active in Anti-HIV Biosynthesis

et al. 2017

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Daurichromenic acid (DCA) synthase catalyzes the oxidative cyclization of grifolic acid to produce DCA, an anti-HIV meroterpenoid isolated from We identified a novel cDNA encoding DCA synthase by transcriptome-based screening from young leaves of The gene coded for a 533-amino acid polypeptide with moderate homologies to flavin adenine dinucleotide oxidases from other plants. The primary structure contained an amino-terminal signal peptide and conserved amino acid residues to form bicovalent linkage to the flavin adenine dinucleotide isoalloxazine ring at histidine-112 and cysteine-175. In addition, the recombinant DCA synthase, purified from the culture supernatant of transgenic , exhibited structural and functional properties as a flavoprotein. The reaction mechanism of DCA synthase characterized herein partly shares a similarity with those of cannabinoid synthases from, whereas DCA synthase catalyzes a novel cyclization reaction of the farnesyl moiety of a meroterpenoid natural product of plant origin. Moreover, in this study, we present evidence that DCA is biosynthesized and accumulated specifically in the glandular scales, on the surface of plants, based on various analytical studies at the chemical, biochemical, and molecular levels. The extracellular localization of DCA also was confirmed by a confocal microscopic analysis of its autofluorescence. These data highlight the unique feature of DCA: the final step of biosynthesis is completed in apoplastic space, and it is highly accumulated outside the scale cells.

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“…2A). Likewise, oxygen removal by either the glucose oxidase-catalase (GO-CAT) system (18,19) To determine the rate of oxygen dissociation from the di-iron center, the GO-CAT system was used to scavenge released oxygen from Td ODP; spectral changes associated with O 2 release were followed at 590 nm (SI Appendix, Fig. S3F).…”

Section: Significancementioning

confidence: 99%

A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species

Muok

Deng

Gumerov

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Many bacteria contain cytoplasmic chemoreceptors that lack sensor domains. Here, we demonstrate that such cytoplasmic receptors found in 8 different bacterial and archaeal phyla genetically couple to metalloproteins related to β-lactamases and nitric oxide reductases. We show that this oxygen-binding di-iron protein (ODP) acts as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable μ-peroxo adduct. Crystal structures of ODP from Td and the thermophile Thermotoga maritima (Tm) in the Fe[III]2-O22−, Zn[II], and apo states display differences in subunit association, conformation, and metal coordination that indicate potential mechanisms for sensing. In reconstituted systems, iron-peroxo ODP destabilizes the phosphorylated form of the receptor-coupled histidine kinase CheA, thereby providing a biochemical link between oxygen sensing and chemotaxis in diverse prokaryotes, including anaerobes of ancient origin.

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Simple Method of Anaerobic Cultivation, with Removal of Oxygen by a Buffered Glucose Oxidase-Catalase System

Cited by 15 publications

References 0 publications

Cannabidiolic‐acid synthase, the chemotype‐determining enzyme in the fiber‐type Cannabis sativa

Cannabidiolic‐acid synthase, the chemotype‐determining enzyme in the fiber‐type Cannabis sativa

Identification and Characterization of Daurichromenic Acid Synthase Active in Anti-HIV Biosynthesis

A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species

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