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Literature summary extracted from

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

Cloned(Commentary)

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.2 Aspergillus niger Q9C2Z0
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.2.2.2 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)

EC Number Purification (Comment) Organism
4.2.2.2 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)

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

Synonyms

EC Number Synonyms Comment Organism
4.2.2.2 pectate lyase A
-
 Aspergillus niger

pI Value

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