Literature summary for 3.2.1.3 extracted from

Dong, Z.Y.; Yang, S.J.; Jin, C.; Zhang, S.Z.
Effect of N-linked oligosaccharide on the conformation and propeties of glucoamylase from Monascus rubiginosus (1996), Ann. N. Y. Acad. Sci., 799, 193-196.

No PubMed abstract available

Search for more literature for 3.2.1.3

Organism

Organism	UniProt	Comment	Textmining
Monascus purpureus	-	enzyme forms E1, E2, E3, E4, E4' and E5	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	enzyme form E3 contains 7% carbohydrate, enzyme form E4 contains 9% carbohydrate, enzyme form E4' contains 2.7% carbohydrate. Degree of N-glycosylation causes the conformational difference between the multiple forms of glucoamylase. Removal of N-linked sugar leeds to a significant thermostability decrease, wheras it has little effect on the catalytic activity	Monascus purpureus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	removal of N-linked sugar led to a significant decrease in thermostability	Monascus purpureus
50	-	2 h, about 50% loss of activity of enzyme form E4', about 15% loss of activity of enzyme form E4	Monascus purpureus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)