ArticleScientific reports2017
Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Microbial inoculants with straw mediate degradation-level-specific changes in soil carbon cycling genes and microbial community.Environmental microbiome · 2026Article
- Production and application of α-amylase, native AmyJ33-ABC, from Bacillus siamensis JJC33M in gelatinized potato starch and its industrial potential.Biotechnology letters · 2025Article
- Genomics and synthetic community experiments uncover the key metabolic roles of acetic acid bacteria in sourdough starter microbiomes.mSystems · 2024Article
- The Distinctive Permutated Domain Structure of Periplasmic α-Amylase (MalS) from Glycoside Hydrolase Family 13 Subfamily 19.Molecules (Basel, Switzerland) · 2023Article
- AmyJ33, a truncated amylase with improved catalytic properties.Biotechnology letters · 2022Article
- Isolation, Extraction, Purification, and Molecular Characterization for ThermostableBiochemistry research international · 2021Article
- Isolation, expression, and characterization of raw starch degrading α-amylase from a marine lakeHeliyon · 2020Article
- Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance.International journal of molecular sciences · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Subfamily 37 of the glycoside hydrolase family GH13 was recently established on the basis of the discovery of a novel α-amylase, designated AmyP, from a marine metagenomic library. AmyP exhibits raw-starch-degrading activity and consists of an N-terminal catalytic domain and a C-terminal starch-binding domain. To understand this newest subfamily, we determined the crystal structure of the catalytic domain of AmyP, named AmyP
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