Functional-genomics-based identification and characterization of open reading frames encoding alpha-glucoside-processing enzymes in the hyperthermophilic archaeon Pyrococcus furiosus.
Bioinformatics analysis and transcriptional response information for Pyrococcus furiosus grown on alpha-glucans led to the identification of a novel isomaltase (PF0132) representing a new glycoside hydrolase (GH) family, a novel GH57 beta-amylase (PF0870), and an extracellular starch-binding protein (1,141 amino acids; PF1109-PF1110), in addition to several other putative alpha-glucan-processing enzymes.
D019295:Computational Biology; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics*; D023281:Genomics / Q000379:methods; D016366:Open Reading Frames / Q000235:genetics*; D020027:Pyrococcus furiosus / Q000201:enzymology* / Q000235:genetics; D000520:alpha-Glucosidases / Q000235:genetics*; D001614:beta-Amylase / Q000235:genetics
D001614:beta-Amylase; D000520:alpha-Glucosidases