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

Identification of the putative proton donor residue of lacto-N-biose phosphorylase (EC 2.4.1.211).

Bioscience, biotechnology, and biochemistry - 1 Jun 2007

Nishimoto Mamoru, Kitaoka Motomitsu

Abstract excerpt

Two lacto-N-biose phosphorylase (LNBP) isozyme genes were cloned from Bifidobacterium bifidum JCM1254. Alignment of the amino acid sequences of LNBP and its homologs identified 24 completely conserved acidic amino acid residues. All single mutants of Bifidobacterium longum LNBP at residues other...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Bifidobacterium
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Isoenzymes

Share to Molecular Sequence Data

Share to Phosphorylases

Share to Protons

Source

Identifiers

PMID: 17587697
DOI: 10.1271/bbb.70064

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17587697-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Identification of the putative proton donor residue of lacto-N-biose phosphorylase (EC 2.4.1.211).PMID 17587697Read ↗

2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.Semantic proximity Read ↗

Sequence analysis of functional regions of homoserine dehydrogenase genes from L-lysine and L-threonine-producing mutants of Brevibacterium lactofermentum.Semantic proximity Read ↗

Unique Sugar Metabolic Pathways of BifidobacteriaSemantic proximity Read ↗

Enhanced production, activity and deregulation of β-galactosidase in a new mutant strain Bifidobacterium longum BIM B-813 D: Characterization and industrial potential.Semantic proximity Read ↗

Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 and comparative physiological studies.Semantic proximity Read ↗

Effect of T- and C-loop mutations on the Herbaspirillum seropedicae GlnB protein in nitrogen signalling.Semantic proximity Read ↗

Safety evaluation of Lactiplantibacillus plantarum N13: genomic, phenotypic, and toxicological assessment for probiotic applications.Semantic proximity Read ↗

Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine.Semantic proximity Read ↗

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