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

Kinetic analysis of Arabidopsis glucosyltransferase UGT74B1 illustrates a general mechanism by which enzymes can escape product inhibition.

The Biochemical journal - 15 Feb 2013

Kopycki Jakub, Wieduwild Elizabeth, Kohlschmidt Janine, Brandt Wolfgang, Stepanova Anna N, Alonso Jose M, Pedras M Soledade C, Abel Steffen, Grubb C Douglas

Abstract excerpt

Plant genomes encode numerous small molecule glycosyltransferases which modulate the solubility, activity, immunogenicity and/or reactivity of hormones, xenobiotics and natural products. The products of these enzymes can accumulate to very high concentrations, yet somehow avoid inhibiting their own biosynthesis. Glucosyltransferase UGT74B1 (UDP-glycosyltransferase 74B1) catalyses the penultimate step in the core...

Read the complete abstract on PubMed

Topics

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

Share to Arabidopsis Proteins
Share to Genome, Plant

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosyltransferases

Share to Kinetics

Share to Leucine

Share to Plants, Genetically Modified

Share to Serine

Share to Substrate Specificity

Source

Identifiers

PMID: 23150922
DOI: 10.1042/BJ20121403

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic analysis of Arabidopsis glucosyltransferase UGT74B1 illustrates a general mechanism by which enzymes can escape product inhibition.PMID 23150922Read ↗

Kinetics of Secoisolariciresinol Glucosyltransferase LuUGT74S1 and Its Mutants.Semantic proximity Read ↗

Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants.Semantic proximity Read ↗

Enzymatic properties of UDP-glycosyltransferase 89B1 from radish and modulation of enzyme catalytic activity via loop region mutation.Semantic proximity Read ↗

Differences in salicylic acid glucose conjugations by UGT74F1 and UGT74F2 from Arabidopsis thaliana.Semantic proximity Read ↗

Comparative analysis of Arabidopsis UGT74 glucosyltransferases reveals a special role of UGT74C1 in glucosinolate biosynthesis.Semantic proximity Read ↗

Histidine 352 (His352) and tryptophan 355 (Trp355) are essential for flax UGT74S1 glucosylation activity toward secoisolariciresinol.Semantic proximity Read ↗

Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate biosynthesis and auxin homeostasis.Semantic proximity Read ↗

Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases.Semantic proximity Read ↗

Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation.Semantic proximity Read ↗

Starch synthases.Semantic proximity Read ↗

Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1.Semantic proximity Read ↗

UDP-glucosyltransferase71c5, a major glucosyltransferase, mediates abscisic acid homeostasis in Arabidopsis.Semantic proximity Read ↗

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