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Literature summary for 1.3.3.6 extracted from

  • Zhang, L.; Li, H.; Gao, L.; Qi, Y.; Fu, W.; Li, X.; Zhou, X.; Gao, Q.; Gao, Z.; Jia, H.
    Acyl-CoA oxidase 1 is involved in gamma-decalactone release from peach (Prunus persica) fruit (2017), Plant Cell Rep., 36, 829-842 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
CoA co-treatment with ACX1 and CoA significantly promoted the biosynthesis of gamma-decalactone compared to the control Prunus persica
additional information exogenous application of recombinant PpACX1 and C16-CoA substrate markedly promots gamma-decalactone biosynthesis, while C16-CoA substrate application alone does not promote its biosynthesis in mesocarp discs cultured in vitro Prunus persica

Cloned(Commentary)

Cloned (Comment) Organism
gene ACX1, real-time quantitative PCR enzyme expression analysis in fruit from the different cultivars, recombinant expression of His-tagged enzyme in from vector pET32a in Escherichia coli Prunus persica

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ no effect on enzyme activity up to 20 mM, inhibitory above, 40% inhibition at 30 mM Prunus persica
Mn2+ has no significant effect on enzyme activity up to 10 mM Prunus persica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten hyperbolic kinetic model Prunus persica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + O2 Prunus persica
-
trans-2,3-dehydroacyl-CoA + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Prunus persica J7K6M3 five cvs., two soft melting peaches Hu Jing Mi Lu and Feng Hua Yu Lu with strong aroma, one hard melting peach Tai Gu Rou Tao with intermediate aroma, and two hard melting peaches Zhong Hua Shou Tao and Zhong Nectarine 16 with slight aroma
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Prunus persica

Source Tissue

Source Tissue Comment Organism Textmining
fruit real-time quantitative PCR enzyme expression analysis in fruit from the different cultivars Prunus persica
-
mesocarp isozyme PpACX1 is the most abundant PpACX protein in fully ripe mesocarp of cultivar Hu Jing Mi Lu Prunus persica
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + O2
-
Prunus persica trans-2,3-dehydroacyl-CoA + H2O2
-
?
additional information PpACX1 exhibits activity with medium- to long-chain fatty acyl-CoAs, equally for C10-CoA to C16-CoA. Isozyme PpACX1 activity using C6-CoA and C10-CoA as substrates is relatively lower and both maintains constant during the reaction time, while a linear activity with C16-CoA substrate is observed Prunus persica ?
-
?

Subunits

Subunits Comment Organism
? x * 94440, recombinant enzyme including the pET32a vector encoding a 20.10 kDa protein, MALDITOF/TOF secondary mass spectrometry, x * 74340, sequence calculation and SDS-PAGE Prunus persica

Synonyms

Synonyms Comment Organism
ACX
-
Prunus persica
acyl-CoA oxidase 1
-
Prunus persica
PpACX1
-
Prunus persica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Prunus persica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Prunus persica

Cofactor

Cofactor Comment Organism Structure
FAD
-
Prunus persica

General Information

General Information Comment Organism
physiological function acyl-CoA oxidase 1 is involved in gamma-decalactone release from Prunus persica fruits. gamma-Decalactone accumulation in peach mesocarp is highly correlated with ACX enzyme activity and natural PpACX1 content. Adding the purified recombinant PpACX1 induces gamma-decalactone biosynthesis in cultured mesocarp discs in vitro Prunus persica