ArticleApplied and environmental microbiology2008
Characterization of ApuB, an extracellular type II amylopullulanase from Bifidobacterium breve UCC2003.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 113 citations in OpenAlex.
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- The therapeutic value of bifidobacteria in cardiovascular disease.NPJ biofilms and microbiomes · 2023Review
- Glycogen-Degrading Activities of Catalytic Domains of α-Amylase and α-Amylase-Pullulanase Enzymes Conserved inJournal of bacteriology · 2023Article
- Genomic and epigenetic landscapes drive CRISPR-based genome editing inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Characterization of a novel type of glycogen-degrading amylopullulanase from Lactobacillus crispatus.Applied microbiology and biotechnology · 2022Article
- Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology.Food science and biotechnology · 2021Review
- Molecular analysis of the replication functions of the bifidobacterial conjugative megaplasmid pMP7017.Microbial biotechnology · 2021Article
- A Resource for Cloning and Expression Vectors Designed for Bifidobacteria: Overview of Available Tools and Biotechnological Applications.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Roles of the Cell Surface Architecture ofFrontiers in microbiology · 2021Review
8 more citing papers are in PubMed but not listed here.
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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The apuB gene of Bifidobacterium breve UCC2003 was shown to encode an extracellular amylopullulanase. ApuB is composed of a distinct N-terminally located alpha-amylase-containing domain which hydrolyzes alpha-1,4-glucosidic linkages in starch and related polysaccharides and a C-terminally located pullulanase-containing domain which hydrolyzes alpha-1,6 linkages in pullulan, allowing the classification of this enzyme as a bifunctional class II pullulanase. A knockout mutation of the apuB gene in B. breve UCC2003 rendered the resulting mutant incapable of growth in medium containing starch, amylopectin, glycogen, or pullulan as the sole carbon and energy source, confirming the crucial physiological role of this gene in starch metabolism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.