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Enzyme Nomenclature
Information on EC 1.11.2.5 - 3-methyl-L-tyrosine peroxygenase
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The expected taxonomic range for this enzyme is: Streptomyces lavendulae
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EC NUMBER 
COMMENTARY 
1.11.2.5
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RECOMMENDED NAME
GeneOntology No.
3-methyl-L-tyrosine peroxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-methyl-L-tyrosine + H2O2 = 3-hydroxy-5-methyl-L-tyrosine + H2O
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
3-methyl-L-tyrosine:hydrogen-peroxide oxidoreductase (3-hydroxy-5-methyl-L-tyrosine-forming)
The heme-containing peroxygenase from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
physiological function
-
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
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-
?
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
the enzyme catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyl-L-tyrosine
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-
?
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
-
-
?
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
the enzyme catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyl-L-tyrosine
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
B0CN28
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
-
-
?
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
B0CN28
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
a heme containing protein. The conserved motif HXXXC is crucial for heme binding. SfmD binds one molecular of heme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 39800, SDS-PAGE; x * 39854, calculated from sequence (without cofactor)
?
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x * 39800, SDS-PAGE; x * 39854, calculated from sequence (without cofactor)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal His8-tagged SfmD is overexpressed in Escherichia coli BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H313A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine. Heme content of the mutant enzyme is very low, very little heme-Fe binding ability
H317A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine. Heme content of the mutant enzyme is very low, very little heme-Fe binding ability
H191A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine
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H274A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine
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H313A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine. Heme content of the mutant enzyme is very low, very little heme-Fe binding ability
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H317A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine. Heme content of the mutant enzyme is very low, very little heme-Fe binding ability
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LINKS TO OTHER DATABASES (specific for EC-Number 1.11.2.5)
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