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Literature summary for 1.14.14.36 extracted from

  • Halkier, B.A.; Nielsen, H.L.; Koch, B.; Moller B.L.
    Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli (1995), Arch. Biochem. Biophys., 322, 369-377.
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Sorghum bicolor
various N-terminal modifications Sorghum bicolor

Protein Variants

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 [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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Sorghum bicolor 16020
-
microsome
-
Sorghum bicolor
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61700
-
SDS-PAGE Sorghum bicolor
61700
-
calculated from amino acid 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Speharose column chromatography and Reactive Red-120 agarose column chromatography Sorghum bicolor
homogeneity Sorghum bicolor

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0233
-
-
Sorghum bicolor
49.2
-
-
Sorghum bicolor

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CYP79
-
Sorghum bicolor
Cytochrome P450Tyr
-
Sorghum bicolor
P450Tyr
-
Sorghum bicolor
tyrosine N-hydroxylase
-
Sorghum bicolor

Turnover Number [1/s]

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

Cofactor Comment Organism Structure
NADPH
-
Sorghum bicolor