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Literature summary for 1.11.1.13 extracted from

  • Ding, Y.; Cui, K.; Guo, Z.; Cui, M.; Chen, Y.
    Manganese peroxidase mediated oxidation of sulfamethoxazole integrating the computational analysis to reveal the reaction kinetics, mechanistic insights, and oxidation pathway (2021), J. Hazard. Mater., 415, 125719 .
    View publication on PubMed
Search for more literature for 1.11.1.13

Application

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

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/ Products (Substrates)

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
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 2 Mn(III) + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-
Phanerodontia chrysosporium BKMF-1767
-
-
-
Phanerodontia chrysosporium CCTCC AF96007
-
-
-

Reaction

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
a

Source Tissue

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
MnP
-
 Phanerodontia chrysosporium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme
-
 Phanerodontia chrysosporium

General Information

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