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Literature summary for 1.14.14.39 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 1.14.14.39

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae Lotus japonicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.7
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
0.7
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus
1.7
-
 L-valine 28°C, pH 7.5 Lotus japonicus
1.8
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
1.8
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus
2.6
-
 L-valine 28°C, pH 7.5 Lotus japonicus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Lotus japonicus
-
-

Organism

Organism UniProt Comment Textmining
Lotus japonicus Q6J540
-
-
Lotus japonicus Q6J540 isoform CYP79D4
-
Lotus japonicus Q6J541
-
-
Lotus japonicus Q6J541 isoform CYP79D3
-

Source Tissue

Source Tissue Comment 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 the aerial parts of the plant Lotus japonicus
-
additional information exclusively expressed in aerial parts Lotus japonicus
-
additional information exclusively expressed in root Lotus japonicus
-
root
-
 Lotus japonicus
-
stem
-
 Lotus japonicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 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 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 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 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 Lotus japonicus ?
-
 ?

Synonyms

Synonyms Comment Organism
CYP79D3
-
 Lotus japonicus
CYP79D4
-
 Lotus japonicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.73
-
 L-valine 28°C, pH 7.5 Lotus japonicus
0.83
-
 L-valine 28°C, pH 7.5 Lotus japonicus
2
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
2
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus
3.67
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
3.67
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus

General Information

General Information Comment Organism
physiological function 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
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 28°C, pH 7.5 Lotus japonicus
0.43
-
 L-valine 28°C, pH 7.5 Lotus japonicus
2
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus
2.03
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
2.85
-
 L-isoleucine 28°C, pH 7.5 Lotus japonicus
2.85
-
 L-isoleucine pH 7.5, 28°C Lotus japonicus