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Literature summary extracted from

  • Libbesen, O.; Koch, B.; Halkier, B.A.; Moller, B.L.
    Isolation of the heme-thiolate enzyme chytochrome P-450tyr, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench (1994), Proc. Natl. Acad. Sci. USA, 91, 9740-9744.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.36 microsome
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Sorghum bicolor
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Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.36 57000
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SDS-PAGE Sorghum bicolor

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.36 Sorghum bicolor
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-
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Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.36 combined use of Renex 690, CHAPS and RTX-100 is optimal for maximal recovery and avoidance of conversion into cytochrome P-420 Sorghum bicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.36 L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] high substrate specificity Sorghum bicolor N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
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pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.14.14.36 7 9.5
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Sorghum bicolor