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Literature summary extracted from

  • Naidu, G.S.N.; Panda, T.
    Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach (1999), Enzyme Microb. Technol., 25, 116-124.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.10 Aspergillus niger
-
-
-
4.2.2.10 Aspergillus niger NCIM 548
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.2.10 [6-O-methyl-alpha-D-GalpA]n = [6-O-methyl-alpha-D-GalpA]m + 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosy-[6-O-methyl-alpha-D-GalpA]n-m-1 favours pectin, the methylester, over pectate, the anion, which is the preferred substrate of EC 4.2.2.2, pectate lyase. Demethylation progressively slows its action, it can nevertheless cleave on either side of a demethylated residue if the residue at the other end of the scissile bond is methylated Aspergillus niger
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.10 pectin
-
 Aspergillus niger ?
-
 ?
4.2.2.10 pectin
-
 Aspergillus niger NCIM 548 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.10 pectinlyase
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.2.10 35
-
-
 Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.2.10 4.8
-
-
 Aspergillus niger