Any feedback?
Literature summary for 3.2.1.15 extracted from
- A novel bifunctional pectinase from Penicillium oxalicum SX6 with separate pectin methylesterase and polygalacturonase catalytic domains (2014), Appl. Microbiol. Biotechnol., 98, 5019-5028.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of the wild-type full-length enzyme and its catalytic domain of polygalacturonase in Pichia pastoris strain GS115 | Penicillium oxalicum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | slight inhibition | Penicillium oxalicum |  |
| Ag+ | strong inhibition | Penicillium oxalicum | |
| Ca2+ | - |
Penicillium oxalicum | |
| Co2+ | - |
Penicillium oxalicum | |
| Cr3+ | - |
Penicillium oxalicum | |
| Cu2+ | - |
Penicillium oxalicum | |
| EDTA | - |
Penicillium oxalicum | |
| Fe3+ | slight inhibition | Penicillium oxalicum | |
| K+ | - |
Penicillium oxalicum | |
| Li+ | - |
Penicillium oxalicum | |
| Mg2+ | - |
Penicillium oxalicum | |
| Mn2+ | slight inhibition | Penicillium oxalicum | |
| Na+ | - |
Penicillium oxalicum | |
| Ni2+ | - |
Penicillium oxalicum | |
| Pb2+ | strong inhibition | Penicillium oxalicum | |
| SDS | - |
Penicillium oxalicum | |
| Zn2+ | - |
Penicillium oxalicum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Penicillium oxalicum | - |
isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China | - |
| Penicillium oxalicum SX6 | - |
isolated from acidic wastewater sample (pH 3.0) collected from a tin mine in Yunnan province, China | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | N-glycosylation, deglycosylation by endo-beta-N-acetylglucosaminidase H | Penicillium oxalicum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| pectin + H2O | citrus pectin | Penicillium oxalicum | ? | - |
? | |
| pectin + H2O | citrus pectin | Penicillium oxalicum SX6 | ? | - |
? | |
| polygalacturonic acid + H2O | - |
Penicillium oxalicum | ? | - |
? | |
| polygalacturonic acid + H2O | - |
Penicillium oxalicum SX6 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Penicillium oxalicum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | activity range, profile overview | Penicillium oxalicum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 552.3 | - |
Pectin | pH 5.0, 50°C, recombinant wild-type full-length enzyme | Penicillium oxalicum | |
| 2022 | - |
polygalacturonic acid | pH 5.0, 50°C, recombinant catalytic polygalacturonase domain | Penicillium oxalicum | |
| 4068 | - |
polygalacturonic acid | pH 5.0, 50°C, recombinant wild-type full-length enzyme | Penicillium oxalicum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Penicillium oxalicum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 6 | activity range, profile overview | Penicillium oxalicum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, loss of 50% activity after 1 h | Penicillium oxalicum |
| 3.5 | 6 | purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, completely stable at | Penicillium oxalicum |
| 8 | - |
purified recombinant wild-type full-length enzyme and catalytic domain of polygalacturonase, 37°C, inactivation after 1 h | Penicillium oxalicum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the glycoside hydrolase family GH28 | Penicillium oxalicum |
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
