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

Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases.

The Journal of biological chemistry - 4 Jul 2003

Verdoucq Lionel, Czjzek Mirjam, Moriniere Jeanne, Bevan David R, Esen Asim

Abstract excerpt

Plant beta-glucosidases display varying substrate specificities. The maize beta-glucosidase isozyme Glu1 (ZmGlu1) hydrolyzes a broad spectrum of substrates in addition to its natural substrate DIMBOA-Glc (2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxaxin-3-one), whereas the sorghum beta-glucosidase isozyme Dhr1 (SbDhr1) hydrolyzes exclusively its natural substrate dhurrin...

Read the complete abstract on PubMed

Topics

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

Share to beta-Glucosidase
Share to Binding Sites
Share to Isoenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Plant Proteins

Share to Protein Conformation

Share to Sequence Alignment

Share to Substrate Specificity

Share to Zea mays

Source

Identifiers

PMID: 12684498
DOI: 10.1074/jbc.M301978200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases.PMID 12684498Read ↗

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

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

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

Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases.Semantic proximity Read ↗

Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides.Semantic proximity Read ↗

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

Two sequence elements of glycosyltransferases involved in urdamycin biosynthesis are responsible for substrate specificity and enzymatic activity.Semantic proximity Read ↗

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.Semantic proximity Read ↗

Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger.Semantic proximity Read ↗

Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3-1,4-Glucans through Distinct Mechanisms.Semantic proximity Read ↗

Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from Talaromyces leycettanus JCM12802 by Rational Design.Semantic proximity Read ↗

Free energy-guided Q302P mutation in GH1 β-glucosidase from Aspergillus fumigatus improves enzyme function via catalytic tunnel perturbation.Semantic proximity Read ↗

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