1.11.1.16: versatile peroxidase

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For detailed information about versatile peroxidase, go to the full flat file.

Word Map on EC 1.11.1.16

1.11.1.16

lignin

pleurotus

peroxidases

ligninolytic

eryngii

laccase

white-rot

bjerkandera

ostreatus

veratryl

adusta

chrysosporium

phanerochaete

lignin-degrading

non-phenolic

2,6-dimethoxyphenol

delignification

aryl-alcohols

degradation

synthesis

industry

analysis

paper production

Reaction

1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol

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]

Systematic Name

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Systematic Name on EC 1.11.1.16 - versatile peroxidase

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reactive-black-5:hydrogen-peroxide oxidoreductase

A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].