Results 11 to 20 of about 3,960 (214)

Active Site Loop Dynamics of PriB, a C-prenyltransferase [PDF]

open access: yesStructural Dynamics
Numerous biological functions are demonstrated by prenylated natural compounds, such as prenylated indole analogs. Natural product biosynthesis and modification of structures are significantly influenced by prenyltransferases.
Omowumi Oreoluwa Fagbohun   +1 more
doaj   +3 more sources

Elucidating the Furanocoumarin Biosynthetic Pathway in Apium graveolens L.: Uncovering the Coordination of Core Enzymes in Both Functional Activity and Gene Localization [PDF]

open access: yesPlants
Furanocoumarins and their derivatives are found in various plant species and have attracted considerable attention due to their diverse biological activities. By analyzing the genomes of Apium Graveolens L.
Jiali Zhou   +4 more
doaj   +2 more sources

Structure of bifunctional variediene synthase yields unique insight on biosynthetic diterpene assembly and cyclization [PDF]

open access: yesNature Communications
An unusual family of bifunctional terpene synthases has been identified in which a prenyltransferase assembles 5-carbon precursors to form C20 geranylgeranyl diphosphate (GGPP), which is then converted into a polycyclic product by a cyclase.
Eliott S. Wenger, David W. Christianson
doaj   +2 more sources

The discovery of a key prenyltransferase gene assisted by a chromosome-level Epimedium pubescens genome

open access: yesFrontiers in Plant Science, 2022
Epimedium pubescens is a species of the family Berberidaceae in the basal eudicot lineage, and a main plant source for the traditional Chinese medicine “Herba Epimedii”. The current study achieved a chromosome-level genome assembly of E.
Guoan Shen   +16 more
exaly   +3 more sources

Study of Terpenoid Synthesis and Prenyltransferase in Roots of Rehmannia glutinosa Based on iTRAQ Quantitative Proteomics

open access: yesFrontiers in Plant Science, 2021
Rehmannia glutinosa has important medicinal value; terpenoid is one of the main active components in R. glutinosa. In this study, iTRAQ technique was used to analyze the relative abundance of proteins in roots of R. glutinosa, and 6,752 reliable proteins
Yanqing Zhou, Peilei Chen
exaly   +3 more sources

LaPT2 Gene Encodes a Flavonoid Prenyltransferase in White Lupin

open access: yesFrontiers in Plant Science, 2021
Legume plants are rich in prenylated flavonoid compounds, which play an important role in plant defense and human health. In the present study, we identified a prenyltransferase (PT) gene, named LaPT2, in white lupin (Lupinus albus), which shows a high ...
Wenbo Jiang   +2 more
exaly   +3 more sources

Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis. [PDF]

open access: yesChemistry
This review highlights biocatalytic prenylation as a versatile strategy for tailoring the functional properties of peptides and proteins. By comparing branched isoprenoids with linear lipids, we illustrate how specific prenyl architectures modulate the behaviors of lipidated proteins within membrane environments.
Fujinami D, Ozawa H, Ito S.
europepmc   +2 more sources

Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther

open access: yesMolecules, 2019
A group of prenyltransferases catalyze chain elongation of farnesyl diphosphate (FPP) to designated lengths via consecutive condensation reactions with specific numbers of isopentenyl diphosphate (IPP).
Jyun-Yu Yao   +4 more
doaj   +2 more sources

Biocatalytic access to diverse prenylflavonoids by combining a regiospecific C-prenyltransferase and a stereospecific chalcone isomerase

open access: yesActa Pharmaceutica Sinica B, 2018
Prenylflavonoids are valuable natural products that have diverse biological properties, and are usually generated biologically by multiple metabolic enzymes in nature.
Dawei Chen, Jungui Dai, Ruishan Wang
exaly   +3 more sources

Structure and specificity of a permissive bacterial C-prenyltransferase [PDF]

open access: yesNature Chemical Biology, 2017
This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin.
Elshahawi, Sherif I.   +9 more
openaire   +5 more sources

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