BRENDA - Enzyme Database show
show all sequences of 1.14.14.39

Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus

Forslund, K.; Morant, M.; Jorgensen, B.; Olsen, C.E.; Asamizu, E.; Sato, S.; Tabata, S.; Bak, S.; Plant Physiol. 135, 71-84 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
Lotus japonicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.7
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
1.7
-
L-valine
28C, pH 7.5
Lotus japonicus
1.8
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
2.6
-
L-valine
28C, pH 7.5
Lotus japonicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
;
Lotus japonicus
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lotus japonicus
Q6J540
; isoform CYP79D4
-
Lotus japonicus
Q6J541
; isoform CYP79D3
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
apical leaf, highest enzymic activity among the tissues tested. Also present in the second leaf from top, no transcripts in older leaves
Lotus japonicus
-
additional information
exclusively expressed in aerial parts; exclusively expressed in root; exclusively expressed in the aerial parts of the plant
Lotus japonicus
-
root
-
Lotus japonicus
-
stem
-
Lotus japonicus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
710304
Lotus japonicus
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
710304
Lotus japonicus
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
710304
Lotus japonicus
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
metabolism of L-Leu, L-Phe, or L-Tyr to the corresponding oximes is not detectable in consistence with the absence of cyanogenic glucosides derived from these amino acids. No substrate: L-Trp, L-Met, L-Pro
710304
Lotus japonicus
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
710304
Lotus japonicus
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.73
-
L-valine
28C, pH 7.5
Lotus japonicus
0.83
-
L-valine
28C, pH 7.5
Lotus japonicus
2
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
3.67
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Saccharomyces cerevisiae
Lotus japonicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.7
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
1.7
-
L-valine
28C, pH 7.5
Lotus japonicus
1.8
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
2.6
-
L-valine
28C, pH 7.5
Lotus japonicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Lotus japonicus
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
apical leaf, highest enzymic activity among the tissues tested. Also present in the second leaf from top, no transcripts in older leaves
Lotus japonicus
-
additional information
exclusively expressed in aerial parts; exclusively expressed in the aerial parts of the plant
Lotus japonicus
-
additional information
exclusively expressed in root
Lotus japonicus
-
root
-
Lotus japonicus
-
stem
-
Lotus japonicus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
710304
Lotus japonicus
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
710304
Lotus japonicus
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
710304
Lotus japonicus
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
metabolism of L-Leu, L-Phe, or L-Tyr to the corresponding oximes is not detectable in consistence with the absence of cyanogenic glucosides derived from these amino acids. No substrate: L-Trp, L-Met, L-Pro
710304
Lotus japonicus
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
710304
Lotus japonicus
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.73
-
L-valine
28C, pH 7.5
Lotus japonicus
0.83
-
L-valine
28C, pH 7.5
Lotus japonicus
2
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
3.67
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
General Information
General Information
Commentary
Organism
physiological function
enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus; enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus; enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val; enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val
Lotus japonicus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus; enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val
Lotus japonicus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.32
-
L-valine
28C, pH 7.5
Lotus japonicus
0.43
-
L-valine
28C, pH 7.5
Lotus japonicus
2
-
L-isoleucine
pH 7.5, 28C
Lotus japonicus
2.03
-
L-isoleucine
28C, pH 7.5
Lotus japonicus
2.85
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.32
-
L-valine
28C, pH 7.5
Lotus japonicus
0.43
-
L-valine
28C, pH 7.5
Lotus japonicus
2
-
L-isoleucine
pH 7.5, 28C
Lotus japonicus
2.03
-
L-isoleucine
28C, pH 7.5
Lotus japonicus
2.85
-
L-isoleucine
28C, pH 7.5; pH 7.5, 28C
Lotus japonicus
Other publictions for EC 1.14.14.39
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)
710304
Forslund
Biosynthesis of the nitrile gl ...
Lotus japonicus
Plant Physiol.
135
71-84
2004
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6
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10
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4
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2
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10
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708971
Andersen
Cytochromes P-450 from cassava ...
Manihot esculenta
J. Biol. Chem.
275
1966-1975
2000
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1
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1
1
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2
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7
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1
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1
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1
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1
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2
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1
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1
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