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Literature summary extracted from
- Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli (1995), Arch. Biochem. Biophys., 322, 369-377.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.36 | glutathione | at 3 mM, activation rate differs between experiments | Sorghum bicolor |  |
| 1.14.14.36 | glutathione | 3 mM glutathione stimulates activity of the reconstituted enzyme | Sorghum bicolor | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.36 | expressed in Escherichia coli JM109 cells | Sorghum bicolor |
| 1.14.14.36 | various N-terminal modifications | Sorghum bicolor |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.14.36 | additional information | mutant 1: first codons of Escherichia coli mRNA are enriched for A's and T's, second codon is changed into GCT, first 8 codons of P450 sequence are replaced with the N-terminal sequence of bovine P45017alpha, mutant 2: deletion of 14 amino acids, mutant 3: deletion of 25 amino acids, mutant 4: deletion of 75 amino acids | Sorghum bicolor |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.36 | 0.22 | - |
L-tyrosine | in reconstitution experiments using Sorghum bicolor | Sorghum bicolor | |
| 1.14.14.36 | 0.22 | - |
L-tyrosine | recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.36 | membrane | - |
Sorghum bicolor | 16020 | - |
| 1.14.14.36 | microsome | - |
Sorghum bicolor | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.36 | 61700 | - |
SDS-PAGE | Sorghum bicolor |
| 1.14.14.36 | 61700 | - |
calculated from amino acid sequence | Sorghum bicolor |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.36 | L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] | Sorghum bicolor | enzyme in biosynthesis of cyanogenic glucosides | N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.36 | Sorghum bicolor | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.36 | DEAE-Speharose column chromatography and Reactive Red-120 agarose column chromatography | Sorghum bicolor |
| 1.14.14.36 | homogeneity | Sorghum bicolor |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.36 | 0.0233 | - |
- |
Sorghum bicolor |
| 1.14.14.36 | 49.2 | - |
- |
Sorghum bicolor |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.36 | L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] | - |
Sorghum bicolor | (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O | - |
? | |
| 1.14.14.36 | L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] | overall reaction, P450Tyr is a multifunctional tyrosine N-hydroxylase catalyzing the double N-hydroxylation of L-tyrosine to N,N-dihydroxy-L-tyrosine which dehydrates and decarboxylates to 4-hydroxyphenylacetaldoxime | Sorghum bicolor | (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O | - |
? | |
| 1.14.14.36 | L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] | enzyme in biosynthesis of cyanogenic glucosides | Sorghum bicolor | N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.36 | additional information | P450Tyr does not metabolize L-phenylalanine | Sorghum bicolor | ? | - |
? | |
| 1.14.14.36 | N-hydroxy-L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] | - |
Sorghum bicolor | N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.36 | CYP79 | - |
Sorghum bicolor |
| 1.14.14.36 | Cytochrome P450Tyr | - |
Sorghum bicolor |
| 1.14.14.36 | P450Tyr | - |
Sorghum bicolor |
| 1.14.14.36 | tyrosine N-hydroxylase | - |
Sorghum bicolor |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.36 | 0.82 | - |
L-tyrosine | in reconstitution experiments using Sorghum bicolor | Sorghum bicolor | |
| 1.14.14.36 | 0.82 | - |
L-tyrosine | purified recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor | |
| 1.14.14.36 | 5.83 | - |
L-tyrosine | in E. coli membranes | Sorghum bicolor | |
| 1.14.14.36 | 5.83 | - |
L-tyrosine | unpurified recombinant enzyme in Escherichia coli membranes, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.36 | NADPH | - |
Sorghum bicolor | |
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