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Literature summary extracted from

  • Reading, N.S.; Aust, S.D.
    Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability (2000), Biotechnol. Prog., 16, 326-333.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.11.1.13 environmental protection mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants Phanerodontia chrysosporium
1.11.1.13 paper production mediated system of degradation is potentially valuable for pulp and paper industries Phanerodontia chrysosporium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.13 expression of A48C/A63C double mutant mnp gene in Escherichia coli XL-1 Blue Phanerodontia chrysosporium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.13 crystal structure Phanerodontia chrysosporium

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.13 A48C/A63C A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity Phanerodontia chrysosporium

General Stability

EC Number General Stability Organism
1.11.1.13 calcium stabilizes Phanerodontia chrysosporium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.13 Ca2+ MnP calcium binding site, calcium content: 4 mol per mol of native MnP, 2 mol per mol of recombinant and A48C/A63C double mutant MnP, calcium decreases the rate of thermal inactivation Phanerodontia chrysosporium

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.13 Phanerodontia chrysosporium
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.13 glycoprotein glycosylation stabilizes MnP Phanerodontia chrysosporium

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.13 isoenzyme H4 Phanerodontia chrysosporium
1.11.1.13 purification of recombinant A48C/A63C double mutant MnP, expressed in Escherichia coli Phanerodontia chrysosporium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2
-
 Phanerodontia chrysosporium Mn3+ + H2O
-
 ?
1.11.1.13 additional information structural properties Phanerodontia chrysosporium ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.11.1.13 additional information
-
 susceptible to thermal inactivation due to the loss of calcium, calcium content after thermal treatment at 37°C for 15 min: 1.5 mol per mol of native MnP, 1 mol per mol of recombinant MnP and 1.3 mol per mol of A48C/A63C double mutant MnP, biphasic inactivation kinetics, recombinant MnP is more sensitive than native MnP as a result of the lack of glycosylation, calcium decreases the rate of thermal inactivation and reactivates MnP up to 50% of its original activity, while EGTA increases the rate of inactivation Phanerodontia chrysosporium
1.11.1.13 37
-
 recombinant MnP: 5 min, 50% loss of activity, A48C/A63C double mutant MnP: relatively stable Phanerodontia chrysosporium
1.11.1.13 52
-
 recombinant MnP: 20 s, 50% loss of activity, A48C/A63C double mutant MnP: 2 min, 50% loss of activity Phanerodontia chrysosporium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.13 24
-
 Mn2+ A48C/A63C double mutant MnP after thermal treatment at 37°C for 15 min Phanerodontia chrysosporium
1.11.1.13 218
-
 Mn2+ native MnP Phanerodontia chrysosporium
1.11.1.13 270 273 Mn2+ recombinant MnP and A48C/A63C double mutant MnP Phanerodontia chrysosporium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.11.1.13 additional information
-
 recombinant MnP is more sensitive than native MnP as a result of lack of glycosylation Phanerodontia chrysosporium
1.11.1.13 4.5
-
 recombinant MnP, native MnP and A48C/A63C double mutant MnP are stable Phanerodontia chrysosporium
1.11.1.13 6
-
 native and A48C/A63C double mutant MnP: 1 h, less than 40% loss of activity Phanerodontia chrysosporium
1.11.1.13 7
-
 native MnP: 1 h, 80% loss of activity, A48C/A63C double mutant MnP: 1 h, 60% loss of activity Phanerodontia chrysosporium
1.11.1.13 8
-
 recombinant MnP: inactivation within 1 min, native MnP: inactivation within 15 min, A48C/A63C double mutant MnP: 1 h, 80% loss of activity Phanerodontia chrysosporium

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.13 heme enzyme contains a pentacoordinated, essentially high-spin ferric heme Phanerodontia chrysosporium
1.11.1.13 heme heme protein Phanerodontia chrysosporium