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

Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase.

The Journal of biological chemistry - 30 Nov 2001

van der Veen B A, Leemhuis H, Kralj S, Uitdehaag J C, Dijkstra B W, Dijkhuizen L

Abstract excerpt

Cyclodextrin-glycosyltransferases (CGTases) (EC ) preferably catalyze transglycosylation reactions with glucosyl residues as acceptor, whereas the homologous alpha-amylases catalyze hydrolysis reactions using water as acceptor. This difference in reaction specificity is most likely caused by the acceptor binding site. To investigate this in detail we altered the acceptor site residues Lys-232, Phe-183, Phe-259,...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Glucosyltransferases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutamic Acid

Share to Histidine

Share to Hydrolysis

Share to Lysine

Share to Phenylalanine

Source

Identifiers

PMID: 11555657
DOI: 10.1074/jbc.M107533200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase.PMID 11555657Read ↗

The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 implications for product inhibition and product specificity.Semantic proximity Read ↗

Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans.Semantic proximity Read ↗

Mutations at calcium binding site III in cyclodextrin glycosyltransferase improve β-cyclodextrin specificity.Semantic proximity Read ↗

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.Semantic proximity Read ↗

Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity.Semantic proximity Read ↗

Mutations at subsite -3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity.Semantic proximity Read ↗

The role of histidine residues in the catalytic act of cyclomaltodextrin glucanotransferase from Bacillus circulans var. alkalophilus.Semantic proximity Read ↗

Effect of Leu277 on Disproportionation and Hydrolysis Activity in Bacillus stearothermophilus NO2 Cyclodextrin Glucosyltransferase.Semantic proximity Read ↗

Mutations enhance β-cyclodextrin specificity of cyclodextrin glycosyltransferase from Bacillus circulans.Semantic proximity Read ↗

Maltose binding site 2 mutations affect product inhibition of Bacillus circulans STB01 cyclodextrin glycosyltransferase.Semantic proximity Read ↗

Engineering CGTase to improve synthesis of alkyl glycosides.Semantic proximity Read ↗

Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge.Semantic proximity Read ↗

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