Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

C-Prenylation of dihydrochalcones by prenyltransferases AnaPT and its engineered mutants.

Bioorganic chemistry - 1 Nov 2025

Zhou Qi, Yang Yanzhi, Yu Xia, Yuan Chun-Mao, Zhou Kang

Abstract excerpt

Prenylated dihydrochalcones mainly occur in plants and show various biological activities. In biological systems, the enzymatic introduction of prenyl groups is catalyzed by prenyltransferases. Notably, fungal prenyltransferases exhibit significant substrate promiscuity, accepting diverse aromatic acceptors and utilizing various prenyl donors. In this study, saturation mutagenesis at I266, a key residue in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Molecular Structure
Share to Mutation
Share to Protein Engineering

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 41172781
DOI: 10.1016/j.bioorg.2025.109131

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

C-Prenylation of dihydrochalcones by prenyltransferases AnaPT and its engineered mutants.PMID 41172781Read ↗

Tuning aromatic cage occupancy in prenyltransferases enables selective and efficient production of rare c-prenylated flavonoids.Semantic proximity Read ↗

Characterization of a Prenyltransferase for Iso-A82775C Biosynthesis and Generation of New Congeners of ChloropestolidesSemantic proximity Read ↗

Reprogramming Substrate and Catalytic Promiscuity of Tryptophan Prenyltransferases.Semantic proximity Read ↗

Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines.Semantic proximity Read ↗

Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants.Semantic proximity Read ↗

An aromatic substrate prenyltransferase involved in the chemical diversification of flavonoids in <i>Glycyrrhiza glabra</i>Semantic proximity Read ↗

Determination of residues responsible for substrate and product specificity of Solanum habrochaites short-chain cis-prenyltransferases.Semantic proximity Read ↗

Unearthing a sesterterpene biosynthetic repertoire in the Brassicaceae through genome mining reveals convergent evolution.Semantic proximity Read ↗

A membrane-bound aromatic <i>O</i> -prenyltransferase catalyzes the last reaction step in citrus auraptene biosynthesisSemantic proximity Read ↗

Mutation on Gly115 and Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 increases its catalytic activity toward hydroxynaphthalenes.Semantic proximity Read ↗

Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi.Semantic proximity Read ↗

Templating effects in aristolochene synthase catalysis: elimination versus cyclisation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.