BRENDA - Enzyme Database show
show all sequences of 1.14.14.39

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
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.3
-
L-isoleucine
pH 7.9, 30°C
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
-
-
Manihot esculenta
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Manihot esculenta
Q9M7B7
cf. EC 1.14.14.38
-
Manihot esculenta
Q9M7B8
cf. EC 1.14.14.38
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
recombinant protein expressed in Pichia pastoris is glycosylated
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 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
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
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. 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
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 61200, calculated, x * 62000, SDS-PAGE
Manihot esculenta
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.1
-
L-isoleucine
pH 7.9, 30°C
Manihot esculenta
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Pichia pastoris
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, 30°C
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
-
-
Manihot esculenta
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
recombinant protein expressed in Pichia pastoris is glycosylated
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 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
708971
Manihot esculenta
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
?
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
?
-
-
-
-
additional information
enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. 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
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 61200, calculated, x * 62000, SDS-PAGE
Manihot esculenta
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.1
-
L-isoleucine
pH 7.9, 30°C
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
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
-
-
1
-
-
-
-
4
1
-
-
-
-
6
-
-
-
-
-
4
-
-
10
-
-
-
-
4
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
5
-
-
10
-
-
-
-
4
-
-
-
-
-
1
2
-
5
5
708971
Andersen
Cytochromes P-450 from cassava ...
Manihot esculenta
J. Biol. Chem.
275
1966-1975
2000
-
-
1
-
-
-
-
1
1
-
2
-
-
7
-
1
-
-
-
1
-
-
4
1
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
2
-
2
-
-
-
1
-
-
2
-
-
4
1
-
-
-
1
-
-
-
-
-
1
2
-
-
-