Literature summary for 1.14.14.36 extracted from

Koch, B.M.; Sibbesen, O.; Halkier B.A.; Svendsen, I.; M�ller B.L.
The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench (1995), Arch. Biochem. Biophys., 323, 177-186.

Search for more literature for 1.14.14.36

Cloned(Commentary)

Cloned (Comment)	Organism
full length clone	Sorghum bicolor

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
61760	-	calculated from amino acid sequence	Sorghum bicolor
61890	-	calculated from DNA sequence	Sorghum bicolor

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Sorghum bicolor	Q43135	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
no modification	no posttranslational modifications at the N- and C-terminal ends except for the N-terminal methionine removal	Sorghum bicolor

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]	-	Sorghum bicolor	N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + 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	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)