Information on EC 1.11.1.16 - versatile peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.16
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RECOMMENDED NAME
GeneOntology No.
versatile peroxidase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
manganese oxidation I
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SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY hide
114995-15-2
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42613-30-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 5
H2O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 51
H2O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 360
H2O2
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural changes in the mutants D153H, D153A, R244L, N246H, N246A, D153A/N246A are confined to the distal heme environment
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D153A
mutation minimally affects the second order rate constant for Compound I formation and the specificity constant for H2O2, but substitution dramatically reduces the stability of Compound I
D153A/N246A
mutation reduces the second order rate constant for Compound I formation and the specificity constant for H2O2 less than 30fold, substitution dramatically reduces the stability of Compound I
D153H
mutant is more than an order of magnitude less reactive with H2O2 than wild-type
N246A
mutation inimally affects the second order rate constant for Compound I formation and the specificity constant for H2O2, but substitution dramatically reduces the stability of Compound I
N246H
no detectable peroxidase activity
R244L
mutation abolishes the peroxidase activity, and heme iron of the mutant shows a pH-dependent transition from high spin pH 5 to low spin pH 8.5