Literature summary for 3.2.1.15 extracted from

Van Santen, Y.; Benen, J.A.E.; Schroer, K.H.; Kalk, K.H.; Armand, S.; Visser, J.; Dijkstra, B.W.
1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis (1999), J. Biol. Chem., 274, 30474-30480.

Search for more literature for 3.2.1.15

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Aspergillus niger

Protein Variants

Protein Variants	Comment	Organism
D180E	0.01% of wild type activity, Km-values change minimally	Aspergillus niger
D180N	0.08% of wild type activity, Km-values change minimally	Aspergillus niger
D201E	0.01% of wild type activity, Km-values change minimally	Aspergillus niger
D201N	0.01% of wild type activity, Km-values change minimally	Aspergillus niger
D202E	0.6% of wild type activity, Km-values change minimally	Aspergillus niger
D202N	0.01% of wild type activity, Km-values change minimally	Aspergillus niger
H223A	enzyme has only 0.5% of wild type activity, no effect of Km-value	Aspergillus niger
K258N	0.8% of wild type activity, 10fold decrease in Km-values	Aspergillus niger
R256N	14% of wild type activity, 10fold decrease in Km-values	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
polygalacturonate + H2O	-	Aspergillus niger	oligogalacturonates	-	?

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)