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IUBMB Comments 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.
The enzyme appears in viruses and cellular organisms
Synonyms
3-methyl-L-tyrosine peroxidase, 3-methyltyrosine peroxidase, SacD, SfmD,
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3-methyl-L-tyrosine peroxidase
3-methyltyrosine peroxidase
3-methyl-L-tyrosine peroxidase
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3-methyl-L-tyrosine peroxidase
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3-methyltyrosine peroxidase
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3-methyltyrosine peroxidase
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SacD
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SfmD
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3-methyl-L-tyrosine + H2O2 = 3-hydroxy-5-methyl-L-tyrosine + H2O
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-
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-
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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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3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
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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-
?
L-tyrosine + H2O2 + H+
?
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?
L-tyrosine + H2O2 + H+
?
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-
-
?
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3-methyl-L-tyrosine + H2O2 + H+
3-hydroxy-5-methyl-L-tyrosine + H2O
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 is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
-
-
?
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heme
a heme containing protein. The conserved motif HXXXC is crucial for heme binding. SfmD binds one molecular of heme
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0.63
3-methyl-L-tyrosine
pH 9.0, 25°C
1
L-tyrosine
pH 9.0, 25°C
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0.476
3-methyl-L-tyrosine
pH 9.0, 25°C
0.205
L-tyrosine
pH 9.0, 25°C
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0.76
3-methyl-L-tyrosine
pH 9.0, 25°C
0.205
L-tyrosine
pH 9.0, 25°C
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UniProt
brenda
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UniProt
brenda
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physiological function
the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family
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
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SFMD_STRLA
365
0
38191
Swiss-Prot
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G8JZ12_RHOFA
278
0
30688
TrEMBL
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A0A5E7IWT2_PSEFL
350
0
39014
TrEMBL
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A0A2S0Q5L6_NODSP
193
0
22290
TrEMBL
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A0A2D0IV29_9GAMM
352
0
39936
TrEMBL
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39800
x * 39800, SDS-PAGE
39854
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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x * 39800, SDS-PAGE
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?
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x * 39854, calculated from sequence (without cofactor)
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H191A
mutant loses ability to hydroxylate 3-methyl-L-tyrosine
H274A
mutant loses ability to hydroxylate 3-methyl-L-tyrosine
H313A
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
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
-
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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C-terminal His8-tagged SfmD is overexpressed in Escherichia coli BL21 (DE3)
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Tang, M.C.; Fu, C.Y.; Tang, G.L.
Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis
J. Biol. Chem.
287
5112-5121
2012
Streptomyces lavendulae (B0CN28), Streptomyces lavendulae NRRL 11002 (B0CN28)
brenda
Fu, C.Y.; Tang, M.C.; Peng, C.; Li, L.; He, Y.L.; Liu, W.; Tang, G.L.
Biosynthesis of 3-hydroxy-5-methyl-o-methyltyrosine in the saframycin/safracin biosynthetic pathway
J. Microbiol. Biotechnol.
19
439-446
2009
Streptomyces lavendulae (B0CN28)
brenda
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1.11.2.5 3-methyl-L-tyrosine peroxygenase
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