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Literature summary for 2.5.1.20 extracted from

  • Cornish, K.; Xie, W.
    Natural rubber biosynthesis in plants: rubber transferase (2012), Methods Enzymol., 515, 63-82.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics analysis, overview Helianthus annuus
additional information
-
additional information kinetics analysis, overview Hevea brasiliensis
additional information
-
additional information kinetics analysis, overview Ficus elastica
additional information
-
additional information kinetics analysis, overview Parthenium argentatum
additional information
-
additional information kinetics analysis, overview Taraxacum kok-saghyz
additional information
-
additional information kinetics analysis, overview Euphorbia lactiflua

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm at the surface of cytoplasmic rubber particles Helianthus annuus 5737
-
cytoplasm at the surface of cytoplasmic rubber particles Hevea brasiliensis 5737
-
cytoplasm at the surface of cytoplasmic rubber particles Ficus elastica 5737
-
cytoplasm at the surface of cytoplasmic rubber particles Parthenium argentatum 5737
-
cytoplasm at the surface of cytoplasmic rubber particles Taraxacum kok-saghyz 5737
-
cytoplasm at the surface of cytoplasmic rubber particles Euphorbia lactiflua 5737
-
membrane bound Helianthus annuus 16020
-
membrane bound Hevea brasiliensis 16020
-
membrane bound Ficus elastica 16020
-
membrane bound Parthenium argentatum 16020
-
membrane bound Taraxacum kok-saghyz 16020
-
membrane bound Euphorbia lactiflua 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Helianthus annuus
Mg2+ activates Hevea brasiliensis
Mg2+ activates Ficus elastica
Mg2+ activates Parthenium argentatum
Mg2+ activates Taraxacum kok-saghyz
Mg2+ activates Euphorbia lactiflua

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Parthenium argentatum presence of a single rubber transferase capable of using isopentenyl diphosphate in purified rubber particles ?
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Helianthus annuus
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Hevea brasiliensis
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Ficus elastica
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Parthenium argentatum
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Taraxacum kok-saghyz
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate Euphorbia lactiflua
-
diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?

Organism

Organism UniProt Comment Textmining
Euphorbia lactiflua
-
-
-
Ficus elastica
-
-
-
Helianthus annuus
-
-
-
Hevea brasiliensis
-
-
-
Parthenium argentatum
-
-
-
Taraxacum kok-saghyz
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Parthenium argentatum makes rubber in parenchyma cells, which must be homogenized to release the rubber particles, the method for purification of enzymatically active rubber particles from the plant requires homogenization that also releases copious amounts of proteases and other degradative enzymes, with a resultant decrease in enzyme stability and half-life, overview Parthenium argentatum

Source Tissue

Source Tissue Comment Organism Textmining
parenchyma
-
Parthenium argentatum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information presence of a single rubber transferase capable of using isopentenyl diphosphate in purified rubber particles Parthenium argentatum ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substarte and activator, overview Hevea brasiliensis ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substarte and activator, overview Parthenium argentatum ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substrate and activator, overview Helianthus annuus ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substrate and activator, overview Ficus elastica ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substrate and activator, overview Taraxacum kok-saghyz ?
-
?
additional information assay development for determination of rubber transferase activity in purified rubber particles using photoaffinity-labeled substrate analogues, overview. The molecular weight of the rubber made during in vitro assays is primarily governed by the rate of the chain transfer reaction, that is, the termination and release of an existing rubber polymer molecule, coupled with the initiation of a new molecule in the same active site, the regulation depends strongly upon the identity of substrate and activator, overview Euphorbia lactiflua ?
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Helianthus annuus diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Hevea brasiliensis diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Ficus elastica diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Parthenium argentatum diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Taraxacum kok-saghyz diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?
polycis-polyprenyl diphosphate + isopentenyl diphosphate
-
Euphorbia lactiflua diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
-
?

Synonyms

Synonyms Comment Organism
cis prenyl transferase
-
Helianthus annuus
cis prenyl transferase
-
Hevea brasiliensis
cis prenyl transferase
-
Ficus elastica
cis prenyl transferase
-
Parthenium argentatum
cis prenyl transferase
-
Taraxacum kok-saghyz
cis prenyl transferase
-
Euphorbia lactiflua
rubber transferase
-
Helianthus annuus
rubber transferase
-
Hevea brasiliensis
rubber transferase
-
Ficus elastica
rubber transferase
-
Parthenium argentatum
rubber transferase
-
Taraxacum kok-saghyz
rubber transferase
-
Euphorbia lactiflua

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
16
-
assay at Parthenium argentatum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
enzyme activity in rubber particles purified from line 593 decreases below limits of detection in 1 h at 25°C, whereas activity is stable for much longer in particles from line 11591 Parthenium argentatum

General Information

General Information Comment Organism
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Helianthus annuus
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Hevea brasiliensis
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Ficus elastica
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Parthenium argentatum
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Taraxacum kok-saghyz
metabolism the isoprenoid pathway includes the enzymes that can also compete with rubber transferase for isopentenyl pyrophosphate (monomer), allylic pyrophosphate (initiator), and magnesium ions (activator), overview Euphorbia lactiflua