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Literature summary for 1.14.14.38 extracted from

  • Forslund, K.; Morant, M.; Jorgensen, B.; Olsen, C.E.; Asamizu, E.; Sato, S.; Tabata, S.; Bak, S.
    Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus (2004), Plant Physiol., 135, 71-84.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.38

Cloned(Commentary)

Cloned (Comment) Organism
expression in Lotus japonicus Manihot esculenta
expression in Saccharomyces cerevisiae Lotus japonicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7
-
 L-valine pH 7.5, 28°C Lotus japonicus
2.6
-
 L-valine pH 7.5, 28°C Lotus japonicus

Localization

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

Organism

Organism UniProt Comment Textmining
Lotus japonicus Q6J540 cf. EC 1.14.14.38
-
Lotus japonicus Q6J541 cf. EC 1.14.14.38
-
Manihot esculenta Q9M7B7 isoform CYP79D2
-

Source Tissue

Source Tissue Comment Organism Textmining
aerial part exclusively expressed in aerial parts Lotus japonicus
-
root
-
 Manihot esculenta
-
root exclusively expressed in root Lotus japonicus
-

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-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 Lotus japonicus (E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
 ?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 Lotus japonicus (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
-
 ?
additional information enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39, 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 Lotus japonicus ?
-
 ?

Synonyms

Synonyms Comment Organism
CYP79D3
-
 Lotus japonicus
CYP79D4
-
 Lotus japonicus
N-hydroxylating cytochrome P450
-
 Manihot esculenta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.83
-
 L-valine pH 7.5, 28°C Lotus japonicus
1.23
-
 L-valine pH 7.5, 28°C Lotus japonicus

General Information

General Information Comment Organism
physiological function in Lotus japonicus expressing Manihot esculenta CYP79D2, the the cyanide potential is approximately twice as high as in wild-type plants. While thelinamarin content is increased approximately 20fold, the lotaustralin content is only slightly increased. The ratio of rhodiocyanoside A and D to lotaustralin is unaltered in leaves. In roots expressing cassava CYP79D2, linamarin and lotaustralin can be detected although in much smaller quantities than in green tissue Manihot esculenta
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 Lotus japonicus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.32
-
 L-valine pH 7.5, 28°C Lotus japonicus
0.43
-
 L-valine pH 7.5, 28°C Lotus japonicus