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Literature summary for 1.11.2.5 extracted from
- Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis (2012), J. Biol. Chem., 287, 5112-5121.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| C-terminal His8-tagged SfmD is overexpressed in Escherichia coli BL21 (DE3) | Streptomyces lavendulae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H191A | mutant loses ability to hydroxylate 3-methyl-L-tyrosine | Streptomyces lavendulae |
| H274A | mutant loses ability to hydroxylate 3-methyl-L-tyrosine | Streptomyces lavendulae |
| 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 | Streptomyces lavendulae |
| 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 | Streptomyces lavendulae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.63 | - |
3-methyl-L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae |  |
| 1 | - |
L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 39800 | - |
x * 39800, SDS-PAGE | Streptomyces lavendulae |
| 39854 | - |
x * 39854, calculated from sequence (without cofactor) | Streptomyces lavendulae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-methyl-L-tyrosine + H2O2 + H+ | Streptomyces lavendulae | the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
| 3-methyl-L-tyrosine + H2O2 + H+ | Streptomyces lavendulae NRRL 11002 | the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces lavendulae | B0CN28 | - |
- |
| Streptomyces lavendulae NRRL 11002 | B0CN28 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Streptomyces lavendulae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-methyl-L-tyrosine + H2O2 + H+ | the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family | Streptomyces lavendulae | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
| 3-methyl-L-tyrosine + H2O2 + H+ | the enzyme catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyl-L-tyrosine | Streptomyces lavendulae | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
| 3-methyl-L-tyrosine + H2O2 + H+ | the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family | Streptomyces lavendulae NRRL 11002 | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
| 3-methyl-L-tyrosine + H2O2 + H+ | the enzyme catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyl-L-tyrosine | Streptomyces lavendulae NRRL 11002 | 3-hydroxy-5-methyl-L-tyrosine + H2O | - |
? | |
| L-tyrosine + H2O2 + H+ | - |
Streptomyces lavendulae | ? | - |
? | |
| L-tyrosine + H2O2 + H+ | - |
Streptomyces lavendulae NRRL 11002 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 39800, SDS-PAGE | Streptomyces lavendulae |
| ? | x * 39854, calculated from sequence (without cofactor) | Streptomyces lavendulae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3-methyl-L-tyrosine peroxidase | - |
Streptomyces lavendulae |
| 3-methyltyrosine peroxidase | - |
Streptomyces lavendulae |
| SacD | - |
Streptomyces lavendulae |
| SfmD | - |
Streptomyces lavendulae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Streptomyces lavendulae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.205 | - |
L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae | |
| 0.476 | - |
3-methyl-L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Streptomyces lavendulae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | a heme containing protein. The conserved motif HXXXC is crucial for heme binding. SfmD binds one molecular of heme | Streptomyces lavendulae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family | Streptomyces lavendulae |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.205 | - |
L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae | |
| 0.76 | - |
3-methyl-L-tyrosine | pH 9.0, 25°C | Streptomyces lavendulae | |
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