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

EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
3-methyl-L-tyrosine + H2O2 = 3-hydroxy-5-methyl-L-tyrosine + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
saframycin A biosynthesis
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
show the reaction diagram
L-tyrosine + H2O2 + H+
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
a heme containing protein. The conserved motif HXXXC is crucial for heme binding. SfmD binds one molecular of heme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
3-methyl-L-tyrosine
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pH 9.0, 25°C
1
L-tyrosine
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pH 9.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.476
3-methyl-L-tyrosine
Streptomyces lavendulae
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pH 9.0, 25°C
0.205
L-tyrosine
Streptomyces lavendulae
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pH 9.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76
3-methyl-L-tyrosine
Streptomyces lavendulae
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pH 9.0, 25°C
10920
0.205
L-tyrosine
Streptomyces lavendulae
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pH 9.0, 25°C
109
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39800
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x * 39800, SDS-PAGE
39854
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x * 39854, calculated from sequence (without cofactor)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 hide
LITERATURE
H191A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine
H274A
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mutant loses ability to hydroxylate 3-methyl-L-tyrosine
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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