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Literature summary for 4.2.2.10 extracted from

  • Sanchez-Torres, P.; Visser, J.; Benen, J.A.
    Identification of amino acid residues critical for catalysis and stability in Aspergillus niger family 1 pectin lyase A (2003), Biochem. J., 370, 331-337.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.2.10

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant enzymes in Aspergillus niger strain NW188, subcloning in Escherichia coli DH5alpha Aspergillus niger

Protein Variants

Protein Variants Comment Organism
D154A site-directed mutagenesis, reduced activity compared to the wild-type enzyme Aspergillus niger
D154E site-directed mutagenesis, reduced activity compared to the wild-type enzyme Aspergillus niger
D186N site-directed mutagenesis, reduced activity and altered pH profile compared to the wild-type enzyme Aspergillus niger
D186N/D221N site-directed mutagenesis, reduced activity and altered pH profile compared to the wild-type enzyme Aspergillus niger
D221N site-directed mutagenesis, reduced activity and altered pH profile compared to the wild-type enzyme Aspergillus niger
K239N site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Aspergillus niger
N109A site-directed mutagenesis, reduced activity compared to the wild-type enzyme Aspergillus niger
R176A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Aspergillus niger
R176D site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Aspergillus niger
R176K site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Aspergillus niger
R236A site-directed mutagenesis, active site residue exchange, completely inactive mutant Aspergillus niger
R236K site-directed mutagenesis, active site residue exchange, completely inactive mutant Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of wild-type and mutant enzymes, influence of pH on the kinetics Aspergillus niger

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 x * 45000, SDS-PAGE Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger Q01172 family 1 pectin lyase A
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the wild-type enzyme is N-glycosylated Aspergillus niger

Purification (Commentary)

Purification (Comment) Organism
native wild-type enzyme and recombinant mutant enzymes to homogeneity Aspergillus niger

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, catalytic residues Arg236, Arg176, and Lys239 are essentially involved in catalysis Aspergillus niger
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information pH driven conformational changes of the enzyme, wild-type and mutants Aspergillus niger ?
-
 ?
partially methyl-esterified pectin prepared from citrus and Aspergillus sp. Aspergillus niger ?
-
 ?
pectin citrus pectin Aspergillus niger ?
-
 ?

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Aspergillus niger

Synonyms

Synonyms Comment Organism
family 1 pectin lyase A
-
 Aspergillus niger
PL1A
-
 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
5
-
 mutant D186N Aspergillus niger
6
-
 wild-type enzyme Aspergillus niger
8
-
 mutants D221N and D186N/D221N Aspergillus niger

pH Range

pH Minimum pH Maximum Comment Organism
5 8
-
 Aspergillus niger