Literature summary for 3.2.1.59 extracted from

Gruen, C.H.; Dekker, N.; Nieuwland, A.A.; Klis, F.M.; Kamerling, J.P.; Vliegenthart, J.F.; Hochstenbach, F.
Mechanism of action of the endo-(1->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum (2006), FEBS Lett., 580, 3780-3786.

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Inhibitors

Inhibitors	Comment	Organism	Structure
glucoamylase	strongly decreases activity	Trichoderma harzianum
glucocerebrosidase	strongly decreases activity	Trichoderma harzianum
additional information	periodate oxidation alone reduces MutAp activity to ca. 40% of control values. Deoxynojirimycin, N-methyl deoxynojirimycin, castanospermine, D-glucono-1,5-lactone, conduritol-beta-epoxide, N-(5-adamantane-1-yl-methoxy)pentyldeoxynojirimycin, periodate and borohydride do not inhibit activity	Trichoderma harzianum

Organism

Organism	UniProt	Comment	Textmining
Trichoderma harzianum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Trichoderma harzianum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-1,3-glucan + H2O	MutAp displays endo-hydrolytic activity. A tetrasaccharide is the minimal substrate for MutAp. The polysaccharide-binding domain in MutAp may be involved in processivity, either by partially disrupting the crystalline structure of (1-3)-alpha-glucan and thereby making it more accessible to hydrolysis, or by assisting in retention of (1-3)-alpha-glucan after each round of hydrolysis. The enzyme breaks an intrachain glycosidic linkage of (1-3)-alpha-glucan, and then continues its hydrolysis towards the non-reducing end by releasing beta-glucose residues in a processive manner. Acts by inversion of the anomeric configuration	Trichoderma harzianum	beta-D-glucose + ?	-	?

Synonyms

Synonyms	Comment	Organism
endo-(1-3)-alpha-glucanase	-	Trichoderma harzianum
MutAp	-	Trichoderma harzianum

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Release 2023.1 (January 2023)