ArticleMarine biotechnology (New York, N.Y.)2012
Identification and phylogenetic characterization of a new subfamily of α-amylase enzymes from marine microorganisms.
Article in Marine biotechnology (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- A cold-adapted and detergent-stable α-amylase from marine bacterium Photobacterium gaetbulicola Gung47Applied microbiology and biotechnology · 2026Article
- Blue Biotechnology: Marine Bacteria Bioproducts.Microorganisms · 2024Review
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- Isolation, identification andBiochemistry and biophysics reports · 2018Article
- Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13.Scientific reports · 2017Article
- Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization.Scientific reports · 2016Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
- Purification, crystallization and preliminary crystallographic analysis of the marine α-amylase AmyP.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Biocatalysts and small molecule products from metagenomic studies.Current opinion in chemical biology · 2012Review
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A gene encoding a starch-hydrolyzing enzyme was isolated from a marine metagenomic library and overexpressed in Escherichia coli. The enzyme, designated AmyP, shows very low similarity to full-length sequences of known α-amylases, although a catalytic domain correlated with the α-amylase superfamily was identified. Based on the range of substrate hydrolysis and the product profile, the protein was clearly defined as a saccharifying-type α-amylase. Sequence comparison indicated that AmyP was related to four putative glycosidases previously identified only in bacterial genome sequences. They were all from marine bacteria and formed a new subfamily of glycoside hydrolase GH13. Moreover, this subfamily was closely related to the probable genuine bacterial α-amylases (GH13_19). The results suggested that the subfamily may be an independent clade of ancestral marine bacterial α-amylases.
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Registered trials
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.