BRENDA - Enzyme Database show
show all sequences of 1.14.14.37

Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants

Busk, P.K.; Moller, B.L.; Plant Physiol. 129, 1222-1231 (2002)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Sorghum bicolor
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
Sorghum bicolor
involved in dhurrin synthesis
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sorghum bicolor
-
L. Moench
-
Sorghum bicolor
O48958
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Sorghum bicolor
-
seed
maximal activity after 1 day of germination
Sorghum bicolor
-
stem
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Sorghum bicolor
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
-
660217
Sorghum bicolor
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
involved in dhurrin synthesis
660217
Sorghum bicolor
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Sorghum bicolor
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Sorghum bicolor
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Sorghum bicolor
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
Sorghum bicolor
involved in dhurrin synthesis
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Sorghum bicolor
-
seed
maximal activity after 1 day of germination
Sorghum bicolor
-
stem
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Sorghum bicolor
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
-
660217
Sorghum bicolor
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
involved in dhurrin synthesis
660217
Sorghum bicolor
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
at all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes. During development, the activity of tyrosine N-monooxygenase CYP79A1 is lower than the activity of 4-hydroxyphenylacetaldehyde oxime monooxygenase CYP71E1, suggesting that CYP79A1 catalyzes the rate-limiting step in dhurrin synthesis
Sorghum bicolor
General Information (protein specific)
General Information
Commentary
Organism
physiological function
at all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes. During development, the activity of tyrosine N-monooxygenase CYP79A1 is lower than the activity of 4-hydroxyphenylacetaldehyde oxime monooxygenase CYP71E1, suggesting that CYP79A1 catalyzes the rate-limiting step in dhurrin synthesis
Sorghum bicolor
Other publictions for EC 1.14.14.37
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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739696
Bavishi
Application of nanodisc techno ...
Sorghum bicolor
Sci. Rep.
6
29459
2016
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739318
Clausen
The bifurcation of the cyanoge ...
Sorghum bicolor
Plant J.
84
558-573
2015
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723366
Jensen
Homology modeling of the three ...
Sorghum bicolor
Phytochemistry
72
2113-2123
2011
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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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660216
Nielsen
Leucine-derived cyano glucosid ...
Hordeum vulgare
Plant Physiol.
129
1066-1075
2002
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660217
Busk
Dhurrin synthesis in sorghum i ...
Sorghum bicolor
Plant Physiol.
129
1222-1231
2002
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739341
Bak
Transgenic tobacco and Arabido ...
Sorghum bicolor
Plant Physiol.
123
1437-1448
2000
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390081
Kahn
Substrate specificity of the c ...
Sorghum bicolor
Arch. Biochem. Biophys.
363
9-18
1999
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285333
Bak
Cloning of three A-type cytoch ...
Sorghum bicolor
Plant Mol. Biol.
36
393-405
1998
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739339
Kahn
Isolation and reconstitution o ...
Sorghum bicolor
Plant Physiol.
115
1661-1670
1997
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285332
Shimada
The enzymatic conversion of p- ...
Sorghum bicolor
Arch. Biochem. Biophys.
180
199-207
1977
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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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