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Literature summary for 4.2.2.10 extracted from

  • van Alebeek, G.J.; Christensen, T.M.; Schols, H.A.; Mikkelsen, J.D.; Voragen, A.G.
    Mode of action of pectin lyase A of Aspergillus niger on differently C(6)-substituted oligogalacturonides (2002), J. Biol. Chem., 277, 25929-25936.
    View publication on PubMed
Search for more literature for 4.2.2.10

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information subsite affinities, kinetics Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Aspergillus niger 4M-147
-
-
-

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 reaction mechanism Aspergillus niger
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.9
-
 purified enzyme, acetate buffer 50 mM Aspergillus niger
32
-
 purified enzyme, McIlvaine buffer with 0.1 M citrate and 0.2 M phosphate Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(6-O-CH3-GalpA)4
-
 Aspergillus niger ?
-
 ?
(6-O-CH3-GalpA)4
-
 Aspergillus niger 4M-147 ?
-
 ?
(6-O-CH3-GalpA)5
-
 Aspergillus niger ?
-
 ?
(6-O-CH3-GalpA)5
-
 Aspergillus niger 4M-147 ?
-
 ?
(6-O-CH3-GalpA)6
-
 Aspergillus niger ?
-
 ?
(6-O-CH3-GalpA)6
-
 Aspergillus niger 4M-147 ?
-
 ?
(6-O-CH3-GalpA)7
-
 Aspergillus niger ?
-
 ?
(6-O-CH3-GalpA)7
-
 Aspergillus niger 4M-147 ?
-
 ?
(6-O-CH3-GalpA)8
-
 Aspergillus niger ?
-
 ?
(6-O-CH3-GalpA)9 best substrate Aspergillus niger ?
-
 ?
DELTA4,5-(6-O-CH3-GalpA)4
-
 Aspergillus niger ?
-
 ?
DELTA4,5-(6-O-CH3-GalpA)5
-
 Aspergillus niger ?
-
 ?
DELTA4,5-(6-O-CH3-GalpA)6
-
 Aspergillus niger ?
-
 ?
additional information substrate specificity, activity increases with increasing length of the substrate up to polymerization degree of 8 monomers, enzyme is very specific for fully methyl-esterified oligogalacturonides, removal of the methyl-ester or changing the type of ester, e.g. ethyl esterification, or transamidation result in almost complete loss of activity, enzyme is capable of cleaving the bond between a methyl-esterified and a non-esterified galacturonic acid residue, where the newly formed DELTA4,5 unsaturated non-reducing end residue always contains a methyl-ester, product determination by mass spectrometry Aspergillus niger ?
-
 ?
additional information substrate specificity, activity increases with increasing length of the substrate up to polymerization degree of 8 monomers, enzyme is very specific for fully methyl-esterified oligogalacturonides, removal of the methyl-ester or changing the type of ester, e.g. ethyl esterification, or transamidation result in almost complete loss of activity, enzyme is capable of cleaving the bond between a methyl-esterified and a non-esterified galacturonic acid residue, where the newly formed DELTA4,5 unsaturated non-reducing end residue always contains a methyl-ester, product determination by mass spectrometry Aspergillus niger 4M-147 ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme contains 8 subsites, mapping Aspergillus niger

Synonyms

Synonyms Comment Organism
pectin lyase A
-
 Aspergillus niger
Pla
-
 Aspergillus niger

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Aspergillus niger