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Functional-Genomics-Based Identification and Characterization of Open Reading Frames Encoding α-Glucoside-Processing Enzymes in the Hyperthermophilic Archaeon Pyrococcus furiosus
Author(s) -
Donald A. Comfort,
ChungJung Chou,
Shan B. Conners,
Amy L. VanFossen,
Robert M. Kelly
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01920-07
Subject(s) - pyrococcus furiosus , biochemistry , glycoside hydrolase , biology , open reading frame , enzyme , structural genomics , amylase , gene , chemistry , computational biology , archaea , peptide sequence , protein structure
Bioinformatics analysis and transcriptional response information forPyrococcus furiosus grown on α-glucans led to the identification of a novel isomaltase (PF0132) representing a new glycoside hydrolase (GH) family, a novel GH57 β-amylase (PF0870), and an extracellular starch-binding protein (1,141 amino acids; PF1109-PF1110), in addition to several other putative α-glucan-processing enzymes.

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