KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.14 | - |
L-tyrosine | presence of 0.15 mM NaCl, pH 7.9, 25°C | Sorghum bicolor | |
0.21 | - |
L-tyrosine | pH 7.9, 25°C | Sorghum bicolor |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Sorghum bicolor | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sorghum bicolor | Q43135 | - |
- |
Renatured (Comment) | Organism |
---|---|
lipid micelles made from L-alpha-dilauroyl phosphatidylcholine are more than twice as effective in reconstituting cytochrome P-450Tyr activity as compared to other lipids | 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 | overall reaction | ? | |
additional information | product of the second N-hydroxylation reaction is N,N-dihydroxytyrosine. N,N-dihydroxytyrosine is dehydrated to 2-nitroso-3-(4-hydroxyphenyl) propionic acid which decarboxylates to p-hydroxyphenylacetaldehyde oxime. The dehydration and decarboxylation reactions may proceed non-enzymatically. The E/Z ratio of the p-hydroxyphenylacetaldehyde oxime produced by reconstituted cytochrome P450Tyr is 69:31. Binding of L-tyrosine or N-hydroxytyrosine mutually excludes binding of the other substrate | Sorghum bicolor | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP79A1 | - |
Sorghum bicolor |
Cytochrome P450Tyr | - |
Sorghum bicolor |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.33 | - |
L-tyrosine | presence of 0.15 mM NaCl, pH 7.9, 25°C | Sorghum bicolor | |
3.83 | - |
L-tyrosine | pH 7.9, 25°C | Sorghum bicolor |