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Literature summary extracted from

  • Tu, T.; Bai, Y.; Luo, H.; Ma, R.; Wang, Y.; Shi, P.; Yang, P.; Meng, K.; Yao, B.
    A novel bifunctional pectinase from Penicillium oxalicum SX6 with separate pectin methylesterase and polygalacturonase catalytic domains (2014), Appl. Microbiol. Biotechnol., 98, 5019-5028.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.11 expressed in Pichia pastoris strain GS115 Penicillium oxalicum
3.2.1.15 recombinant expression of the wild-type full-length enzyme and its catalytic domain of polygalacturonase in Pichia pastoris strain GS115 Penicillium oxalicum
3.2.1.67 recombinant expression of the wild-type full-length enzyme and its catalytic domain of polygalacturonase in Pichia pastoris strain GS115 Penicillium oxalicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.11 beta-mercaptoethanol 96% residual activity at 1 mM Penicillium oxalicum
3.2.1.15 2-mercaptoethanol slight inhibition Penicillium oxalicum
3.2.1.15 Ag+ strong inhibition Penicillium oxalicum
3.2.1.15 Ca2+
-
 Penicillium oxalicum
3.2.1.15 Co2+
-
 Penicillium oxalicum
3.2.1.15 Cr3+
-
 Penicillium oxalicum
3.2.1.15 Cu2+
-
 Penicillium oxalicum
3.2.1.15 EDTA
-
 Penicillium oxalicum
3.2.1.15 Fe3+ slight inhibition Penicillium oxalicum
3.2.1.15 K+
-
 Penicillium oxalicum
3.2.1.15 Li+
-
 Penicillium oxalicum
3.2.1.15 Mg2+
-
 Penicillium oxalicum
3.2.1.15 Mn2+ slight inhibition Penicillium oxalicum
3.2.1.15 Na+
-
 Penicillium oxalicum
3.2.1.15 Ni2+
-
 Penicillium oxalicum
3.2.1.15 Pb2+ strong inhibition Penicillium oxalicum
3.2.1.15 SDS
-
 Penicillium oxalicum
3.2.1.15 Zn2+
-
 Penicillium oxalicum
3.2.1.67 2-mercaptoethanol slight inhibition Penicillium oxalicum
3.2.1.67 Ag+ strong inhibition Penicillium oxalicum
3.2.1.67 Ca2+
-
 Penicillium oxalicum
3.2.1.67 Co2+
-
 Penicillium oxalicum
3.2.1.67 Cr3+
-
 Penicillium oxalicum
3.2.1.67 Cu2+
-
 Penicillium oxalicum
3.2.1.67 EDTA
-
 Penicillium oxalicum
3.2.1.67 Fe3+ slight inhibition Penicillium oxalicum
3.2.1.67 K+
-
 Penicillium oxalicum
3.2.1.67 Li+
-
 Penicillium oxalicum
3.2.1.67 Mg2+
-
 Penicillium oxalicum
3.2.1.67 Mn2+ slight inhibition Penicillium oxalicum
3.2.1.67 Na+
-
 Penicillium oxalicum
3.2.1.67 Ni2+
-
 Penicillium oxalicum
3.2.1.67 Pb2+ strong inhibition Penicillium oxalicum
3.2.1.67 SDS
-
 Penicillium oxalicum
3.2.1.67 Zn2+
-
 Penicillium oxalicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.15 additional information
-
 additional information 1.04 mg/ml for the recombinant wild-type full-length enzyme with pectin at pH 5.0, 50°C, 1.79 mg/ml for recombinant wild-type full-length enzyme with polygalacturonic acid at pH 5.0, 50°C, and 1.26 mg/ml for recombinant catalytic polygalacturonase domain with polygalacturonic acid at pH 5.0, 50°C Penicillium oxalicum
3.2.1.67 additional information
-
 additional information 1.79 mg/ml with [(1->4)-alpha-D-galacturonide]n for recombinant wild-type full-length enzyme, and 1.26 mg/ml with [(1->4)-alpha-D-galacturonide]n for recombinant catalytic polygalacturonase domain, pH 5.0, 50°C Penicillium oxalicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.11 Ca2+ 313.2% activity at 1 mM Penicillium oxalicum
3.1.1.11 Co2+ 351.2% activity at 1 mM Penicillium oxalicum
3.1.1.11 Cr3+ 216.5% activity at 1 mM Penicillium oxalicum
3.1.1.11 Cu2+ 104.5% activity at 1 mM Penicillium oxalicum
3.1.1.11 EDTA 229% activity at 1 mM Penicillium oxalicum
3.1.1.11 Fe3+ 107.1% activity at 1 mM Penicillium oxalicum
3.1.1.11 K+ 126.1% activity at 1 mM Penicillium oxalicum
3.1.1.11 Li+ 118.2% activity at 1 mM Penicillium oxalicum
3.1.1.11 Mg2+ 379.5% activity at 1 mM Penicillium oxalicum
3.1.1.11 Mn2+ 369.9% activity at 1 mM Penicillium oxalicum
3.1.1.11 Na+ 137.2% activity at 1 mM Penicillium oxalicum
3.1.1.11 Ni2+ 331.8% activity at 1 mM Penicillium oxalicum
3.1.1.11 Pb2+ 139.2% activity at 1 mM Penicillium oxalicum
3.1.1.11 SDS 105.9% activity at 1 mM Penicillium oxalicum
3.1.1.11 Zn2+ 324.4% activity at 1 mM Penicillium oxalicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.11 38100
-
 x * 38100, calculated from amino acid sequence Penicillium oxalicum
3.1.1.11 55000
-
 x * 55000, SDS-PAGE Penicillium oxalicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.15 additional information Penicillium oxalicum the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 ?
-
 ?
3.2.1.15 additional information Penicillium oxalicum SX6 the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 ?
-
 ?
3.2.1.67 additional information Penicillium oxalicum the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.11 Penicillium oxalicum
-
-
-
3.1.1.11 Penicillium oxalicum SX6
-
-
-
3.2.1.15 Penicillium oxalicum
-
 isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
-
3.2.1.15 Penicillium oxalicum SX6
-
 isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
-
3.2.1.67 Penicillium oxalicum
-
 isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
-
3.2.1.67 Penicillium oxalicum SX6
-
 isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.11 glycoprotein
-
 Penicillium oxalicum
3.2.1.15 glycoprotein N-glycosylation, deglycosylation by endo-beta-N-acetylglucosaminidase H Penicillium oxalicum
3.2.1.67 glycoprotein N-glycosylation, deglycosylation by endo-beta-N-acetylglucosaminidase H Penicillium oxalicum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.11 resource Q column chromatography Penicillium oxalicum
3.2.1.15 recombinant wild-type full-length enzyme and isolated catalytic polygalacturonase domain from Pichia pastoris strain GS115 by ultrafiltration, gel filtration, and anion exchange chromatography, followed by deglycosylation of the proteins by endo-beta-N-acetylglucosaminidase H Penicillium oxalicum
3.2.1.67 recombinant wild-type full-length enzyme and isolated catalytic polygalacturonase domain from Pichia pastoris strain GS115 by ultrafiltration, gel filtration, and anion exchange chromatography, followed by deglycosylation of the proteins by endo-beta-N-acetylglucosaminidase H Penicillium oxalicum

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 68.6
-
 at pH 5.0 and 50°C Penicillium oxalicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.11 citrus pectin + H2O
-
 Penicillium oxalicum methanol + pectate
-
 ?
3.1.1.11 citrus pectin + H2O
-
 Penicillium oxalicum SX6 methanol + pectate
-
 ?
3.1.1.11 sisal fibre + H2O
-
 Penicillium oxalicum ?
-
 ?
3.1.1.11 sisal fibre + H2O
-
 Penicillium oxalicum SX6 ?
-
 ?
3.2.1.15 additional information the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 Penicillium oxalicum ?
-
 ?
3.2.1.15 additional information the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 Penicillium oxalicum SX6 ?
-
 ?
3.2.1.15 pectin + H2O citrus pectin Penicillium oxalicum ?
-
 ?
3.2.1.15 pectin + H2O citrus pectin Penicillium oxalicum SX6 ?
-
 ?
3.2.1.15 polygalacturonic acid + H2O
-
 Penicillium oxalicum ?
-
 ?
3.2.1.15 polygalacturonic acid + H2O
-
 Penicillium oxalicum SX6 ?
-
 ?
3.2.1.67 additional information the enzyme is a bifunctional protein that has both pectin methylesterase, EC 3.1.1.11, and polygalacturonase activities, EC 3.2.1.15 and EC 3.2.1.67, the ratio of pectin methylesterase activity to polygalacturonase activity is about 1:4 Penicillium oxalicum ?
-
 ?
3.2.1.67 [(1->4)-alpha-D-galacturonide]n + H2O
-
 Penicillium oxalicum [(1->4)-alpha-D-galacturonide]n-1 + D-galacturonate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.11 ? x * 55000, SDS-PAGE Penicillium oxalicum
3.1.1.11 ? x * 38100, calculated from amino acid sequence Penicillium oxalicum
3.2.1.15 More the enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase Penicillium oxalicum
3.2.1.67 More the enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase Penicillium oxalicum

Synonyms

EC Number Synonyms Comment Organism
3.1.1.11 pectin methylesterase
-
 Penicillium oxalicum
3.1.1.11 S6PE catalytic domain of pectin methylesterase Penicillium oxalicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.11 50
-
-
 Penicillium oxalicum
3.2.1.15 50
-
-
 Penicillium oxalicum
3.2.1.67 50
-
-
 Penicillium oxalicum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.11 40 55
-
 Penicillium oxalicum
3.2.1.15 30 60 activity range, profile overview Penicillium oxalicum
3.2.1.67 30 60 activity range, profile overview Penicillium oxalicum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.11 40
-
 the enzyme remains stable for 1 h at 40°C Penicillium oxalicum
3.2.1.15 60
-
 purified recombinant proteins, pH 5.0, the wild-type full-length enzyme is completely stable up to, the catalytic domain of polygalacturonase loses 30% within 1 h Penicillium oxalicum
3.2.1.67 60
-
 purified recombinant proteins, pH 5.0, the wild-type full-length enzyme is completely stable up to, the catalytic domain of polygalacturonase loses 30% within 1 h Penicillium oxalicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.11 47.6
-
 citrus pectin at pH 5.0 and 50°C Penicillium oxalicum
3.2.1.15 552.3
-
 Pectin pH 5.0, 50°C, recombinant wild-type full-length enzyme Penicillium oxalicum
3.2.1.15 2022
-
 polygalacturonic acid pH 5.0, 50°C, recombinant catalytic polygalacturonase domain Penicillium oxalicum
3.2.1.15 4068
-
 polygalacturonic acid pH 5.0, 50°C, recombinant wild-type full-length enzyme Penicillium oxalicum
3.2.1.67 2022
-
 [(1->4)-alpha-D-galacturonide]n pH 5.0, 50°C, recombinant catalytic polygalacturonase domain Penicillium oxalicum
3.2.1.67 4068
-
 [(1->4)-alpha-D-galacturonide]n pH 5.0, 50°C, recombinant wild-type full-length enzyme Penicillium oxalicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.11 5
-
-
 Penicillium oxalicum
3.2.1.15 5
-
-
 Penicillium oxalicum
3.2.1.67 5
-
-
 Penicillium oxalicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.11 4 6
-
 Penicillium oxalicum
3.2.1.15 3 6 activity range, profile overview Penicillium oxalicum
3.2.1.67 3 6 activity range, profile overview Penicillium oxalicum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.15 3
-
 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, loss of 50% activity after 1 h Penicillium oxalicum
3.2.1.15 3.5 6 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, completely stable at Penicillium oxalicum
3.2.1.15 8
-
 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, inactivation after 1 h Penicillium oxalicum
3.2.1.67 3
-
 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, loss of 50% activity after 1 h Penicillium oxalicum
3.2.1.67 3.5 6 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, completely stable at Penicillium oxalicum
3.2.1.67 8
-
 purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, inactivation after 1 h Penicillium oxalicum

General Information

EC Number General Information Comment Organism
3.2.1.15 evolution the enzyme belongs to the glycoside hydrolase family GH28 Penicillium oxalicum
3.2.1.15 additional information the multimodular enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase Penicillium oxalicum
3.2.1.67 evolution the enzyme belongs to the glycoside hydrolase family GH28 Penicillium oxalicum
3.2.1.67 additional information the multimodular enzyme consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of polygalacturonase Penicillium oxalicum