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

Natural and recombinant A and B gene encoded glycosyltransferases.

Transfusion medicine (Oxford, England) - 1 Aug 2001

Palcic M M, Seto N O, Hindsgaul O

Abstract excerpt

The human blood group A and B synthesizing enzymes are glycosyltransferases that catalyse the transfer of a monosaccharide residue from UDP-GalNAc and UDP-Gal donors, respectively, to alphaFuc1,2-Gal terminated blood group H acceptors. Extensive investigations of their substrate specificity and physical properties have been carried out since their initial discovery. These studies demonstrated a rigid specificity...

Read the complete abstract on PubMed

Topics

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

Share to ABO Blood-Group System
Share to Carbohydrate Sequence
Share to Forecasting

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Galactosyltransferases

Share to Mammals

Share to N-Acetylgalactosaminyltransferases

Share to Oligosaccharides

Share to Trisaccharides

Source

Identifiers

PMID: 11532187
DOI: 10.1046/j.1365-3148.2001.00314.x

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

Natural and recombinant A and B gene encoded glycosyltransferases.PMID 11532187Read ↗

Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes.Semantic proximity Read ↗

Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli.Semantic proximity Read ↗

Flexibility and mutagenic resiliency of glycosyltransferases.Semantic proximity Read ↗

Amino-acid substitution in the disordered loop of blood group B-glycosyltransferase enzyme causes weak B phenotype.Semantic proximity Read ↗

A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase.Semantic proximity Read ↗

Turning universal O into rare Bombay type blood.Semantic proximity Read ↗

Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B GlycosyltransferasesSemantic proximity Read ↗

Bacterial Homologue of Human Blood Group A TransferaseSemantic proximity Read ↗

Structural basis for red cell phenotypic changes in newly identified, naturally occurring subgroup mutants of the human blood group B glycosyltransferase.Semantic proximity Read ↗

The blood group-specific human glycosyltransferases.Semantic proximity Read ↗

Toward Efficient Enzymes for the Generation of Universal Blood through Structure-Guided Directed Evolution.Semantic proximity Read ↗

Position of human blood group O(H) and phenotype-determining enzymes in growth and infectious disease.Semantic proximity Read ↗

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