BRENDA - Enzyme Database show
show all sequences of 1.14.14.38

Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin: Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes

Andersen, M.D.; Busk, P.K.; Svendsen, I.; Moller, B.L.; J. Biol. Chem. 275, 1966-1975 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Pichia pastoris; expression in Pichia pastoris
Manihot esculenta
Inhibitors
Inhibitors
Commentary
Organism
Structure
diphenyleneiodonium chloride
;
Manihot esculenta
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.3
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
2.2
-
L-valine
pH 7.9, 30C
Manihot esculenta
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
;
Manihot esculenta
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61200
-
-
Manihot esculenta
62000
-
x * 62000, SDS-PAGE and calculated
Manihot esculenta
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Manihot esculenta
Q9M7B7
-
-
Manihot esculenta
Q9M7B8
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
glycosylation of the asparagine residues at the N-terminus; recombinant protein expressed in Pichia pastoris is glycosylated
Manihot esculenta
Purification (Commentary)
Commentary
Organism
recombinant enzyme, reconstitution in lipid micelles; recombinant enzyme, reconstitution in lipid micelles
Manihot esculenta
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
;
Manihot esculenta
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
708971
Manihot esculenta
?
-
-
-
-
additional information
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
708971
Manihot esculenta
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
708971
Manihot esculenta
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 61200, calculated, x * 62000, SDS-PAGE; x * 62000, SDS-PAGE and calculated
Manihot esculenta
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at; assay at
Manihot esculenta
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.103
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
0.16
-
L-valine
pH 7.9, 30C
Manihot esculenta
0.162
-
L-valine
pH 7.9, 30C
Manihot esculenta
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.9
-
assay at; assay at
Manihot esculenta
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Pichia pastoris
Manihot esculenta
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diphenyleneiodonium chloride
-
Manihot esculenta
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.3
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
2.2
-
L-valine
pH 7.9, 30C
Manihot esculenta
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Manihot esculenta
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61200
-
-
Manihot esculenta
62000
-
x * 62000, SDS-PAGE and calculated
Manihot esculenta
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
glycosylation of the asparagine residues at the N-terminus; recombinant protein expressed in Pichia pastoris is glycosylated
Manihot esculenta
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme, reconstitution in lipid micelles
Manihot esculenta
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Manihot esculenta
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
708971
Manihot esculenta
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
708971
Manihot esculenta
?
-
-
-
-
additional information
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
708971
Manihot esculenta
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
708971
Manihot esculenta
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 61200, calculated, x * 62000, SDS-PAGE; x * 62000, SDS-PAGE and calculated
Manihot esculenta
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Manihot esculenta
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.103
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
0.16
-
L-valine
pH 7.9, 30C
Manihot esculenta
0.162
-
L-valine
pH 7.9, 30C
Manihot esculenta
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.9
-
assay at
Manihot esculenta
General Information
General Information
Commentary
Organism
physiological function
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava; bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava. CYP79D1 has a higher kcat value with L-valine as substrate than with L-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava
Manihot esculenta
General Information (protein specific)
General Information
Commentary
Organism
physiological function
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava. CYP79D1 has a higher kcat value with L-valine as substrate than with L-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava
Manihot esculenta
physiological function
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava
Manihot esculenta
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.074
-
L-valine
pH 7.9, 30C
Manihot esculenta
0.1
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.074
-
L-valine
pH 7.9, 30C
Manihot esculenta
0.1
-
L-isoleucine
pH 7.9, 30C
Manihot esculenta
Other publictions for EC 1.14.14.38
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)
728480
Kannangara
Characterization and expressio ...
Manihot esculenta
Plant J.
68
287-301
2011
-
-
-
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710305
Jorgensen
Cassava plants with a depleted ...
Manihot esculenta, Manihot esculenta MCol22
Plant Physiol.
139
363-374
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
710288
Siritunga
Engineering cyanogen synthesis ...
Manihot esculenta
Plant Mol. Biol.
56
661-669
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
710304
Forslund
Biosynthesis of the nitrile gl ...
Lotus japonicus, Manihot esculenta
Plant Physiol.
135
71-84
2004
-
-
2
-
-
-
-
2
1
-
-
-
-
3
-
-
-
-
-
3
-
-
6
-
-
-
-
2
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
3
-
-
6
-
-
-
-
2
-
-
-
-
-
2
3
-
2
2
710302
Mikkelsen
Metabolic engineering of valin ...
Manihot esculenta
Plant Physiol.
131
773-779
2003
-
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
708971
Andersen
Cytochromes P-450 from cassava ...
Manihot esculenta
J. Biol. Chem.
275
1966-1975
2000
-
-
1
-
-
-
1
2
1
-
2
-
-
2
-
1
1
-
-
1
-
-
10
1
1
-
-
3
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
2
2
-
2
-
-
-
1
2
-
2
-
-
10
1
2
-
-
3
2
-
-
-
-
1
2
-
2
2