Literature summary extracted from

Liu, M.; Li, P.; Liu, B.; Su, J.; Wang, C.
Insights into the working mechanism and unfolding property of Arthrobacter chlorophenolicus amylosucrase (2013), Prog. Biochem. Biophys., 40, 565-577.

No PubMed abstract available

General Stability

EC Number	General Stability	Organism
2.4.1.4	the enzyme is quite instable	Pseudarthrobacter chlorophenolicus

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.4.1.4	sucrose + [(1->4)-alpha-D-glucosyl]n	Pseudarthrobacter chlorophenolicus	-	D-fructose + [(1->4)-alpha-D-glucosyl]n+1	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.4	Pseudarthrobacter chlorophenolicus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.4.1.4	additional information	in presence of an activator polymer , in vitro, the enzyme is capable to caalyze the synthesis of an amylose-like polysaccharide composed of only alpha-1,4-linkages using sucrose as the only energy source	Pseudarthrobacter chlorophenolicus	?	-	?
2.4.1.4	sucrose + [(1->4)-alpha-D-glucosyl]n	-	Pseudarthrobacter chlorophenolicus	D-fructose + [(1->4)-alpha-D-glucosyl]n+1	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.4.1.4	More	structure homology modeling based on the crystal structures of Neisseria poylsaccharea and Deinococcus geothermalis, structural differences and dynamics. The enzyme from Arthrobacter chlorophenolicus can be divided into two regions of different moving directions, predicted unfolding pathway, overview	Pseudarthrobacter chlorophenolicus

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.1.4	ACAS	-	Pseudarthrobacter chlorophenolicus

General Information

EC Number	General Information	Comment	Organism
2.4.1.4	evolution	the enzyme belongs to the glycoside hydrolase family GH13	Pseudarthrobacter chlorophenolicus

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Release 2023.1 (January 2023)