PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18552192-1	2008	AmyA, an alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima, is able to hydrolyze internal alpha-1,4-glycosidic bonds in various alpha-glucans at 85 degrees C as the optimal temperature.	alpha-glucans	149-162	alpha-amylase	Thermotoga maritima MSB8	9-22
31190240-1	2019	AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular alpha-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism.	maltodextrin	171-183	alpha-amylase	Thermotoga maritima MSB8	132-145
31190240-1	2019	AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular alpha-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism.	Polysaccharides	207-221	alpha-amylase	Thermotoga maritima MSB8	132-145
31190240-2	2019	However, the alpha-amylase specificity of AmyC is questionable as extensive phylogenetic analysis of GH57 and tertiary structural comparison suggest that AmyC could actually be a glycogen-branching enzyme (GBE), a key enzyme in the biosynthesis of glycogen.	Glycogen	179-187	alpha-amylase	Thermotoga maritima MSB8	13-26
31190240-3	2019	This communication presents phylogenetic and biochemical evidence that AmyC is a GBE with a relatively high hydrolytic (alpha-amylase) activity (up to 30% of the total activity), creating a branched alpha-glucan with 8.5% alpha-1,6-glycosidic bonds.	alpha-glucan	199-211	alpha-amylase	Thermotoga maritima MSB8	120-133