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Literature summary for 1.11.1.13 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure Phanerodontia chrysosporium

Protein Variants

Protein Variants Comment Organism
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

General Stability Organism
calcium stabilizes Phanerodontia chrysosporium

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein glycosylation stabilizes MnP Phanerodontia chrysosporium

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
37
-
recombinant MnP: 5 min, 50% loss of activity, A48C/A63C double mutant MnP: relatively stable Phanerodontia chrysosporium
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]

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

pH Stability

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

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