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

Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity.

Applied microbiology and biotechnology - 1 Mar 2012

Li Yanhong, Yu Hai, Cao Hongzhi, Muthana Saddam, Chen Xi

Abstract excerpt

Cytidine 5'-monophosphate (CMP)-sialic acid synthetases (CSSs) catalyze the formation of CMP-sialic acid from CTP and sialic acid, a key step for sialyltransferase-catalyzed biosynthesis of sialic acid-containing oligosaccharides and glycoconjugates. More than 50 different sialic acid forms have been identified in nature. To facilitate the enzymatic synthesis of sialosides with diverse naturally occurring sialic...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Neisseria meningitidis

Share to Pasteurella multocida

Share to Sequence Alignment

Share to Substrate Specificity

Source

Identifiers

PMID: 21968653
DOI: 10.1007/s00253-011-3579-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity.PMID 21968653Read ↗

A semi-multifunctional sialyltransferase from Bibersteinia trehalosi and its comparison to the Pasteurella multocida ST1 mutants.Semantic proximity Read ↗

Decreasing the sialidase activity of multifunctional Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis.Semantic proximity Read ↗

A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating LewisX.Semantic proximity Read ↗

Cloning and characterization of sialidases with 2-6' and 2-3' sialyl lactose specificity from Pasteurella multocida.Semantic proximity Read ↗

The group B streptococcal sialic acid O-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters.Semantic proximity Read ↗

Highly efficient biosynthesis of 3'-sialyllactose in engineered Escherichia coli.Semantic proximity Read ↗

The capsule polymerase CslB of Neisseria meningitidis serogroup L catalyzes the synthesis of a complex trimeric repeating unit comprising glycosidic and phosphodiester linkages.Semantic proximity Read ↗

CpsK of Streptococcus agalactiae exhibits alpha2,3-sialyltransferase activity in Haemophilus ducreyi.Semantic proximity Read ↗

Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.Semantic proximity Read ↗

Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates.Semantic proximity Read ↗

Arg314 is essential for catalysis by N-acetyl neuraminic acid synthase from Neisseria meningitidis.Semantic proximity Read ↗

Sialylation of lipooligosaccharides is dispensable for the virulence of Haemophilus ducreyi in humans.Semantic proximity Read ↗

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