BRENDA - Enzyme Database show
show all sequences of 1.14.14.36

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

Koch, B.M.; Sibbesen, O.; Halkier B.A.; Svendsen, I.; Möller B.L.; Arch. Biochem. Biophys. 323, 177-186 (1995)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
full length clone
Sorghum bicolor
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61760
-
calculated from amino acid sequence
Sorghum bicolor
61890
-
calculated from DNA sequence
Sorghum bicolor
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Sorghum bicolor
Q43135
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
-
390079
Sorghum bicolor
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
390079
Sorghum bicolor
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
enzyme in biosynthesis of cyanogenic glucosides
390079
Sorghum bicolor
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
full length clone
Sorghum bicolor
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61760
-
calculated from amino acid sequence
Sorghum bicolor
61890
-
calculated from DNA sequence
Sorghum bicolor
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
Sorghum bicolor
enzyme in biosynthesis of cyanogenic glucosides
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
-
390079
Sorghum bicolor
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
390079
Sorghum bicolor
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
enzyme in biosynthesis of cyanogenic glucosides
390079
Sorghum bicolor
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
Other publictions for EC 1.14.14.36
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736574
Gnanasekaran
Transfer of the cytochrome P45 ...
Sorghum bicolor
J. Exp. Bot.
67
2495-2506
2016
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1
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739696
Bavishi
Application of nanodisc techno ...
Sorghum bicolor
Sci. Rep.
6
29459
2016
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1
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4
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1
1
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739318
Clausen
The bifurcation of the cyanoge ...
Sorghum bicolor
Plant J.
84
558-573
2015
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1
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1
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4
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3
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4
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4
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1
1
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660383
Kristensen
Metabolic engineering of dhurr ...
Sorghum bicolor
Proc. Natl. Acad. Sci. USA
102
1779-1784
2005
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1
-
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-
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6
-
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660217
Busk
Dhurrin synthesis in sorghum i ...
Sorghum bicolor
Plant Physiol.
129
1222-1231
2002
-
-
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3
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2
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2
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1
1
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739340
Nielsen
Cloning and expression of cyto ...
Triglochin maritima
Plant Physiol.
122
1311-1321
2000
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1
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6
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1
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739341
Bak
Transgenic tobacco and Arabido ...
Sorghum bicolor
Plant Physiol.
123
1437-1448
2000
-
1
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5
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390081
Kahn
Substrate specificity of the c ...
Sorghum bicolor
Arch. Biochem. Biophys.
363
9-18
1999
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1
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2
1
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1
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4
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1
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4
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1
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1
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1
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4
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390082
Bak
The presence of CYP79 homologu ...
Sinapis alba
Plant Mol. Biol.
38
725-734
1998
-
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1
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11
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1
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739339
Kahn
Isolation and reconstitution o ...
Sorghum bicolor
Plant Physiol.
115
1661-1670
1997
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1
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390079
Koch
The primary sequence of cytoch ...
Sorghum bicolor
Arch. Biochem. Biophys.
323
177-186
1995
-
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1
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2
1
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6
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390080
Halkier
Purification and characterizat ...
Sorghum bicolor
Arch. Biochem. Biophys.
322
369-377
1995
1
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1
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1
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1
2
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1
1
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5
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1
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2
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5
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2
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1
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1
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1
1
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1
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2
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1
1
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1
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2
-
5
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2
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738563
Sibbesen
Cytochrome P-450TYR is a multi ...
Sorghum bicolor
J. Biol. Chem.
270
3506-3511
1995
-
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2
1
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2
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2
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390078
Libbesen
Isolation of the heme-thiolate ...
Sorghum bicolor
Proc. Natl. Acad. Sci. USA
91
9740-9744
1994
-
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1
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1
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348459
Halkier
The biosynthesis of cyanogenic ...
Sorghum bicolor
J. Biol. Chem.
265
21114-21121
1990
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1
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6
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2
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1
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1
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6
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1
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285331
McFarlane
Conn, E.E.: The in vitro biosy ...
Sorghum bicolor
J. Biol. Chem.
250
4708-4713
1975
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