1.11.1.16: versatile peroxidase

This is an abbreviated version!
For detailed information about versatile peroxidase, go to the full flat file.

Reaction

Synonyms

B-type dye-decolorizing peroxidase, bacterial lignin peroxidase, DypB, manganese peroxidase 4, Mb peroxidase, metMb peroxidase, Mnp4, More, myoglobin, R1B4, versatile peroxidase, versatile peroxidase MnP2, versatile peroxidase VPL2 precursor, VP1, Vpl2, VPS1

ECTree

     1 Oxidoreductases

         1.11 Acting on a peroxide as acceptor

             1.11.1 Peroxidases

                1.11.1.16 versatile peroxidase

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Results	in table
2	Activating Compound
33	AA Sequence
27	Application
2	CAS Registry Number
20	Cloned(Commentary)
19	Cofactor
8	Crystallization (Commentary)
1	Expression
36	General Information
14	Inhibitors
165	kcat/KM [mM/s]
291	KM Value [mM]
15	Localization
22	Metals/Ions
12	Molecular Weight [Da]
35	Natural Substrates/ Products (Substrates)
98	Organism
1	Pathway
28	PDB ID
52	pH Optimum
4	pH Range
1	pH Stability
8	pI Value
9	Posttranslational Modification
83	Protein Variants
18	Purification (Commentary)
8	Reaction
78	Reference
3	Renatured (Commentary)
16	Source Tissue
21	Specific Activity [micromol/min/mg]
3	Storage Stability
253	Substrates and Products (Substrate)
20	Subunits
29	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
2	Temperature Range [°C]
7	Temperature Stability [°C]
245	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.11.1.16 - versatile peroxidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

construction of enzyme model and identification of active sites for oxidation of Mn2+ and of aromatic substrates

Bjerkandera adusta

A5JTV4

685634

hanging drop vapor diffusion method, crystal structures of untreated versatile peroxidase (immediately after expression in Escherichia coli and in vitro reconstitution), native versatile peroxidase (treated with Mn2+), D175A variant, and wild-type verstile peroxidase (from Pleurotus eryngii culture)

Pleurotus eryngii

O94753

672267

mutant enzyme W164Y, sitting-drop vapor diffusion method, resolution 1.94 A

Pleurotus eryngii

O94753

704630

mutants E140G, P141G, K176G, and E140G/K176G, to 1.6, 2.0, 1.5, 1.7 and 2.35 A resolution, respectively

Pleurotus eryngii

O94753

725499

sitting drop vapor diffusion method, using 0.1 M sodium MES buffer at pH 6.5, 25% (w/v) PEG 4000 and 0.2 M MgCl2

Pleurotus eryngii

O94753

743592

wild-type and mutant M247F

Pleurotus eryngii

O94753

685203

resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the five-coordinated quantum mechanically mixed-spin state being the most populated in the latter. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -260 mV

Pseudomonas putida

-

724379

structural changes in the mutants D153H, D153A, R244L, N246H, N246A, D153A/N246A are confined to the distal heme environment

Rhodococcus jostii

Q0SE24

725465