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Literature summary for 1.11.1.13 extracted from

  • Kishi, K.; Hildebrand, D.P.; Kusters-van Someren, M.; Gettemy, J.; Mauk, A.G.; Gold, M.H.
    Site-directed mutations at phenylalanine-190 of manganese peroxidase: Effects on stability, function, and coordination (1997), Biochemistry, 36, 4268-4277.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
mutant genes F190Y, F190L, F190I and F190A are subcloned and expressed in Escherichia coli XL-1 Blue and DH5alphaF’ Phanerodontia chrysosporium

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure Phanerodontia chrysosporium

Protein Variants

Protein Variants Comment Organism
F190A mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP Phanerodontia chrysosporium
F190I mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP Phanerodontia chrysosporium
F190L rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP Phanerodontia chrysosporium
F190Y engineered mutant Phanerodontia chrysosporium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.039
-
H2O2 wild-type MnP1 Phanerodontia chrysosporium
0.039 0.041 H2O2 MnP1 from mutants F190Y, F190L, F190I and F190A Phanerodontia chrysosporium
0.074 0.08 Mn2+ MnP1 from mutants F190Y, F190L, F190I and F190A Phanerodontia chrysosporium
0.083
-
Mn2+ wild-type MnP1 Phanerodontia chrysosporium
0.42
-
ferrocyanide MnP1 from mutant F190A Phanerodontia chrysosporium
0.42
-
ferrocyanide mutant enzyme F190A, at pH 4.5 and 25°C Phanerodontia chrysosporium
3.4 3.8 ferrocyanide MnP1 from mutants F190Y, F190L, F190I Phanerodontia chrysosporium
3.4 3.8 ferrocyanide mutant enzyme F190I, at pH 4.5 and 25°C Phanerodontia chrysosporium
3.5
-
ferrocyanide wild-type MnP1 Phanerodontia chrysosporium
3.5
-
ferrocyanide mutant enzyme F190L, at pH 4.5 and 25 °C Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
-
Phanerodontia chrysosporium

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-
Phanerodontia chrysosporium
-
MnP1
-
Phanerodontia chrysosporium
-
auxotrophic strain OGC107-1
-
Phanerodontia chrysosporium OGC101
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of MnPs from the mutants F190Y, F190L, F190I and F190A Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocyanide + H+ + H2O2
-
Phanerodontia chrysosporium ferricyanide + H2O
-
r
ferrocyanide + H+ + H2O2
-
Phanerodontia chrysosporium OGC101 ferricyanide + H2O
-
r
Mn2+ + H+ + H2O2 unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179 Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes lignin ?
Mn2+ + H+ + H2O2 unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179 Phanerodontia chrysosporium OGC101 Mn3+ + H2O Mn3+ oxidizes lignin ?
additional information catalytic cycle with oxidized intermediates MnP compound I and II Phanerodontia chrysosporium ?
-
?
additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium ?
-
?
additional information catalytic cycle with oxidized intermediates MnP compound I and II Phanerodontia chrysosporium OGC101 ?
-
?
additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium OGC101 ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
49
-
wild-type MnP, MnP F190Y and MnP F190L: 330 s, 50% loss of activity, MnP F190I: 30 s, 50% loss of activity, MnP F190A: 5 s, complete loss of activity Phanerodontia chrysosporium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4 4.2 ferrocyanide MnP1 from mutants F190Y, F190L, F190I Phanerodontia chrysosporium
4
-
ferrocyanide wild-type MnP1 Phanerodontia chrysosporium
14.6
-
ferrocyanide MnP1 from mutant F190A Phanerodontia chrysosporium
240 290 Mn2+ MnP1 from mutants F190Y, F190L, F190I and F190A Phanerodontia chrysosporium
290
-
Mn2+ wild-type MnP1 Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition Phanerodontia chrysosporium