Application | Comment | Organism |
---|---|---|
environmental protection | the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance | Phanerodontia chrysosporium |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diphosphate | diphosphate, as a Mn(III) complexing agent can negatively influence the oxidation capacity of Mn3+, which is used to verify the contribution of Mn3+ and other active species to the degradation of SMX | Phanerodontia chrysosporium | |
H2O2 | at high concentrations | Phanerodontia chrysosporium |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 Mn(II) + 2 H+ + H2O2 | Phanerodontia chrysosporium | - |
2 Mn(III) + 2 H2O | - |
? | |
2 Mn(II) + 2 H+ + H2O2 | Phanerodontia chrysosporium CCTCC AF96007 | - |
2 Mn(III) + 2 H2O | - |
? | |
2 Mn(II) + 2 H+ + H2O2 | Phanerodontia chrysosporium BKMF-1767 | - |
2 Mn(III) + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | - |
- |
- |
Phanerodontia chrysosporium BKMF-1767 | - |
- |
- |
Phanerodontia chrysosporium CCTCC AF96007 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O | the proton-coupled electron transfer (PCET) process dominates the catalytic circle of MnP and the transformation of Mn3+, density functional theory (DFT) calculations, overview. During the reaction of H2O2 in the active MnP system, a typical signal of DMPO-Mn3+ is observed, indicating that MnP catalyzes Mn2+ to Mn3+ | Phanerodontia chrysosporium |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | production of ligninolytic enzyme MnP in liquid fermentation medium of Phanerochaete chrysosporium strain BKMF-1767 | Phanerodontia chrysosporium | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
425 U/l of MnP is extracted from the liquid fermentation medium of Phanerochaete chrysosporium and exhibits an efficient catalytic performance for SMX transformation. Optimal activity when the external parameters are designed at pH 5.0, an enzyme activity above 40 U/l, and an H2O2 concentration of 0.2 mM | Phanerodontia chrysosporium |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 Mn(II) + 2 H+ + H2O2 | - |
Phanerodontia chrysosporium | 2 Mn(III) + 2 H2O | - |
? | |
2 Mn(II) + 2 H+ + H2O2 | - |
Phanerodontia chrysosporium CCTCC AF96007 | 2 Mn(III) + 2 H2O | - |
? | |
2 Mn(II) + 2 H+ + H2O2 | - |
Phanerodontia chrysosporium BKMF-1767 | 2 Mn(III) + 2 H2O | - |
? | |
additional information | manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer | Phanerodontia chrysosporium | ? | - |
- |
|
additional information | manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer | Phanerodontia chrysosporium CCTCC AF96007 | ? | - |
- |
|
additional information | manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer | Phanerodontia chrysosporium BKMF-1767 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
MnP | - |
Phanerodontia chrysosporium |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Phanerodontia chrysosporium |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Phanerodontia chrysosporium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Phanerodontia chrysosporium |
General Information | Comment | Organism |
---|---|---|
physiological function | manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate | Phanerodontia chrysosporium |