Literature summary for 2.4.1.25 extracted from

Tafazoli, S.; Wong, A.W.; Akiyama, T.; Kajiura, H.; Tomioka, E.; Kojima, I.; Takata, H.; Kuriki, T.
Safety evaluation of amylomaltase from Thermus aquaticus (2010), Regul. Toxicol. Pharmacol., 57, 62-69.

Search for more literature for 2.4.1.25

Application

Application	Comment	Organism
synthesis	the recombinant enzyme is used to enzymatically-synthesized glycogen as a food ingredient	Thermus aquaticus

Cloned(Commentary)

Cloned (Comment)	Organism
gene malQ, expression in Bacillus subtilis strain NCIMB12378	Thermus aquaticus

Organism

Organism	UniProt	Comment	Textmining
Thermus aquaticus	-	gene malQ	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyzes an inter-molecular transglycosylation, by transfer of alpha glucan moiety from one alpha-1,4-glucan molecule to another or to glucose, forming two linear products of different sizes	Thermus aquaticus	?	-	?

Synonyms

Synonyms	Comment	Organism
amylomaltase	-	Thermus aquaticus
More	amylomaltase is a member of the 4-alpha-glucanotransferase family	Thermus aquaticus
MQ-01	-	Thermus aquaticus

General Information

General Information	Comment	Organism
additional information	MQ-01 fails to exhibit mutagenic activity and does not display clastogenic properties in Chinese hamster lung fibroblast cells. In a 13-week subchronic toxicity study in rats, oral administration of MQ-01 at doses of up to 15 ml/kg body weight/day do not produce compound-related clinical signs or toxicity, changes in body weight gain, food consumption, hematology, clinical chemistry, urinalysis, organ weights, or in any gross and microscopic findings, overview	Thermus aquaticus

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Release 2023.1 (January 2023)