Literature summary for 4.2.2.2 extracted from

Benen, J.A.; Kester, H.C.; Parenicova, L.; Visser, J.
Characterization of Aspergillus niger pectate lyase A (2000), Biochemistry, 39, 15563-15569.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed using a promoter fusion with the Aspergillus niger pyruvate kinase promoter	Aspergillus niger

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	strong sigmoidal CaCl2 concentration dependent relation. Optimal catalysis at 0.5-1.0 mM Ca2+	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	Q9C2Z0	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	purification of the recombinant enzyme results in identification of two enzyme forms of which one appears to be N-glycosylated and the other appears to be free of N-glycosylation. The two enzyme forms show identical specific activies	Aspergillus niger

Purification (Commentary)

Purification (Comment)	Organism
purification of the recombinant enzyme results in identification of two enzyme forms of which one appears to be N-glycosylated and the other appears to be free of N-glycosylation	Aspergillus niger

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
polygalacturonic acid	-	Aspergillus niger	DELTA4,5-unsaturated oligogalacturonides	-	?

Synonyms

Synonyms	Comment	Organism
pectate lyase A	-	Aspergillus niger

pI Value

Organism	Comment	pI Value Maximum	pI Value
Aspergillus niger	calculation from nucleotide sequence	-	4.4

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Release 2023.1 (January 2023)