Bioinformatic and biochemical analysis of a novel maltose-forming α-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1

•We found two maltose-forming α-amylase subgroups in Thermococcus genera.•CL1_0868 (TCMA) is the first maltose-forming α-amylase characterized from Thermococcus species.•TCMA displays dual hydrolysis activity toward α-1,4- and α-1,6-glycosidic linkages and only recognizes maltose.•TCMA displays diff...

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Veröffentlicht in:	Enzyme and microbial technology 2014-06, Vol.60, p.9-15
Hauptverfasser:	Jeon, Eun-Jung, Jung, Jong-Hyun, Seo, Dong-Ho, Jung, Dong-Hyun, Holden, James F., Park, Cheon-Seok
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Amylases - chemistry alpha-Amylases - genetics alpha-Amylases - metabolism Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Cloning, Molecular Computational Biology Escherichia coli Genes, Archaeal Glycoside hydrolase family 57 (GH57) Hyperthermophile Kinetics Maltose - metabolism Maltose-forming α-amylase Molecular Sequence Data Phylogeny Pyrococcus Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid Substrate Specificity Thermococcus Thermococcus - enzymology Thermococcus - genetics Thermococcus sp. CL1
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