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Literature summary extracted from

  • Zhang, Z.; Dong, J.; Zhang, D.; Wang, J.; Qin, X.; Liu, B.; Xu, X.; Zhang, W.; Zhang, Y.
    Expression and characterization of a pectin methylesterase from Aspergillus niger ZJ5 and its application in fruit processing (2018), J. Biosci. Bioeng., 126, 690-696 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.11 gene pme-zj5a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression in Pichia pastoris strain GS115 to 71.11 U/ml after induction with methanol for 20 h at 30°C Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.11 3.27
-
 Pectin recombinant enzyme, pH 3.8, 37°C Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.11 pectin + n H2O Aspergillus niger
-
 n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O Aspergillus niger ZJ5
-
 n methanol + pectate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.11 Aspergillus niger A0A345K402
-
-
3.1.1.11 Aspergillus niger ZJ5 A0A345K402
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.11 glycoprotein the enzyme contains three putative O-glycosylation sites and one N-glycosylation site Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.11 recombinant enzyme from Pichia pastoris strain GS115 Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.11 4.36
-
 purified recombinant enzyme, pH 3.8, 37°C Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.11 additional information generally PMEs from fungal have broad substrate specificity because the methyl groups on pectin are attacked by these enzymes in a random manner. Enzyme PME-ZJ5A shows significant potential for increasing the clarity of pineapple juice Aspergillus niger ?
-
 ?
3.1.1.11 additional information generally PMEs from fungal have broad substrate specificity because the methyl groups on pectin are attacked by these enzymes in a random manner. Enzyme PME-ZJ5A shows significant potential for increasing the clarity of pineapple juice Aspergillus niger ZJ5 ?
-
 ?
3.1.1.11 pectin + n H2O
-
 Aspergillus niger n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O substrates are citrus pectin with 77% methyl-esterified (DE77) and citrus pectin with 85% methyl-esterified (DE85) Aspergillus niger n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O
-
 Aspergillus niger ZJ5 n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O substrates are citrus pectin with 77% methyl-esterified (DE77) and citrus pectin with 85% methyl-esterified (DE85) Aspergillus niger ZJ5 n methanol + pectate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.11 ? x * 37000, recombinant enzyme, SDS-PAGE, x * 34800, sequence calculation Aspergillus niger
3.1.1.11 More the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8 Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.1.1.11 pectin methylesterase
-
 Aspergillus niger
3.1.1.11 PME
-
 Aspergillus niger
3.1.1.11 pme-zj5a
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.11 45
-
-
 Aspergillus niger

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.11 10 60 over 60% of maximal activity at 10-40°C, 25% at 5°C and 60°C, maximal activity at 45°C, inactivation at 65°C Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.11 10 20 purified recombinant enzyme, pH 3.8, 1 h, completely stable Aspergillus niger
3.1.1.11 35 50 purified recombinant enzyme, pH 3.8, 1 h, about 50% activity remaining Aspergillus niger
3.1.1.11 55 60 purified recombinant enzyme, pH 3.8, 1 h, about 20% activity remaining Aspergillus niger

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.11 22.33
-
 Pectin recombinant enzyme, pH 3.8, 37°C Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.11 3.8
-
-
 Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.11 3.3 4.2 over 70% of maximal activity within this range Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.11 2 6.5 purified recombinant enzyme, 37°C, 1 h, over 80% activity remaining Aspergillus niger
3.1.1.11 5
-
 purified recombinant enzyme, 37°C, 1 h, completely stable at Aspergillus niger
3.1.1.11 7 8 purified recombinant enzyme, 37°C, 1 h, about 20% activity remaining Aspergillus niger

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.11 Aspergillus niger sequence calculation
-
 4.2

General Information

EC Number General Information Comment Organism
3.1.1.11 evolution the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8 Aspergillus niger