Activating Compound | Comment | Organism | Structure |
---|---|---|---|
glutathione | at 3 mM, activation rate differs between experiments | Sorghum bicolor | |
glutathione | 3 mM glutathione stimulates activity of the reconstituted enzyme | Sorghum bicolor |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli JM109 cells | Sorghum bicolor |
various N-terminal modifications | Sorghum bicolor |
Protein Variants | Comment | Organism |
---|---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
L-tyrosine | in reconstitution experiments using Sorghum bicolor | Sorghum bicolor | |
0.22 | - |
L-tyrosine | recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Sorghum bicolor | 16020 | - |
microsome | - |
Sorghum bicolor | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
61700 | - |
SDS-PAGE | Sorghum bicolor |
61700 | - |
calculated from amino acid sequence | Sorghum bicolor |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Sorghum bicolor | - |
- |
- |
Purification (Comment) | Organism |
---|---|
DEAE-Speharose column chromatography and Reactive Red-120 agarose column chromatography | Sorghum bicolor |
homogeneity | Sorghum bicolor |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0233 | - |
- |
Sorghum bicolor |
49.2 | - |
- |
Sorghum bicolor |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] | - |
Sorghum bicolor | (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O | - |
? | |
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 | - |
? | |
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] | enzyme in biosynthesis of cyanogenic glucosides | Sorghum bicolor | N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
additional information | P450Tyr does not metabolize L-phenylalanine | Sorghum bicolor | ? | - |
? | |
N-hydroxy-L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] | - |
Sorghum bicolor | N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP79 | - |
Sorghum bicolor |
Cytochrome P450Tyr | - |
Sorghum bicolor |
P450Tyr | - |
Sorghum bicolor |
tyrosine N-hydroxylase | - |
Sorghum bicolor |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.82 | - |
L-tyrosine | in reconstitution experiments using Sorghum bicolor | Sorghum bicolor | |
0.82 | - |
L-tyrosine | purified recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor | |
5.83 | - |
L-tyrosine | in E. coli membranes | Sorghum bicolor | |
5.83 | - |
L-tyrosine | unpurified recombinant enzyme in Escherichia coli membranes, in 50 mM Tricine, pH 7.9, a 30°C | Sorghum bicolor |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Sorghum bicolor |