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Literature summary for 4.2.2.10 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
Search for more literature for 4.2.2.10

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Aspergillus niger NCIM 548
-
-
-

Reaction

Reaction Comment Organism Reaction ID
[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)

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

Synonyms

Synonyms Comment Organism
pectinlyase
-
 Aspergillus niger

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
-
 Aspergillus niger