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Literature summary for 1.14.14.38 extracted from

  • Andersen, M.D.; Busk, P.K.; Svendsen, I.; Moller, B.L.
    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 (2000), J. Biol. Chem., 275, 1966-1975.
    View publication on PubMed
Search for more literature for 1.14.14.38

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Manihot esculenta

Inhibitors

Inhibitors Comment Organism Structure
diphenyleneiodonium chloride
-
 Manihot esculenta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3
-
 L-isoleucine pH 7.9, 30°C Manihot esculenta
2.2
-
 L-valine pH 7.9, 30°C Manihot esculenta

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Manihot esculenta
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61200
-
-
 Manihot esculenta
62000
-
 x * 62000, SDS-PAGE and calculated Manihot esculenta

Organism

Organism UniProt Comment Textmining
Manihot esculenta Q9M7B7
-
-
Manihot esculenta Q9M7B8
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein glycosylation of the asparagine residues at the N-terminus Manihot esculenta
glycoprotein recombinant protein expressed in Pichia pastoris is glycosylated Manihot esculenta

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, reconstitution in lipid micelles Manihot esculenta

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Manihot esculenta
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
 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 Manihot esculenta (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
 ?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 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
-
 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 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 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 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 Manihot esculenta ?
-
 ?

Subunits

Subunits Comment Organism
? x * 62000, SDS-PAGE and calculated Manihot esculenta
? x * 61200, calculated, x * 62000, SDS-PAGE Manihot esculenta

Synonyms

Synonyms Comment Organism
CYP79D1
-
 Manihot esculenta
CYP79D2
-
 Manihot esculenta
N-hydroxylating cytochrome P450
-
 Manihot esculenta
valine N-monooxygenase
-
 Manihot esculenta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Manihot esculenta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.103
-
 L-isoleucine pH 7.9, 30°C Manihot esculenta
0.16
-
 L-valine pH 7.9, 30°C Manihot esculenta
0.162
-
 L-valine pH 7.9, 30°C Manihot esculenta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
 assay at Manihot esculenta

General Information

General Information Comment 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 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. 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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.074
-
 L-valine pH 7.9, 30°C Manihot esculenta
0.1
-
 L-isoleucine pH 7.9, 30°C Manihot esculenta