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Literature summary for 2.5.1.117 extracted from

  • Sadre, R.; Frentzen, M.; Saeed, M.; Hawkes, T.
    Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis (2010), J. Biol. Chem., 285, 18191-18198.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.117

Inhibitors

Inhibitors Comment Organism Structure
haloxydine almost complete inhibition at 0.5 mM. Haloxydine inhibition is uncompetitive with respect to farnsyl diphosphate and either mixed or competitive with respect to homogentisate Arabidopsis thaliana
haloxydine almost complete inhibition at 0.5 mM. Haloxydine inhibition is uncompetitive with respect to farnsyl diphosphate and either mixed or competitive with respect to homogentisate Chlamydomonas reinhardtii
haloxydine almost complete inhibition at 0.5 mM. Haloxydine inhibition is uncompetitive with respect to farnsyl diphosphate and either mixed or competitive with respect to homogentisate Spinacia oleracea
[2-((R)-1-phenyl-ethylamino)-1-phosphono-ethyl]-phosphonic acid structural analogue and inhibitory mimic of farnesyl diphosphate Chlamydomonas reinhardtii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
 (2E,6E)-farnesyl diphosphate pH 8.5, 28°C Chlamydomonas reinhardtii
0.04
-
 homogentisate pH 8.5, 28°C Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Chlamydomonas reinhardtii 16020
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q1ACB3
-
-
Chlamydomonas reinhardtii A1JHN0
-
-
Spinacia oleracea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + homogentisate
-
 Chlamydomonas reinhardtii diphosphate + (3-(2E,6E)-farnesyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
farnesyl diphosphate + homogentisate
-
 Spinacia oleracea diphosphate + (3-(2E,6E)-farnesyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
farnesyl diphosphate + homogentisate
-
 Arabidopsis thaliana diphosphate + (3-(2E,6E)-farnesyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranyl diphosphate + homogentisate
-
 Spinacia oleracea diphosphate + (3-geranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranyl diphosphate + homogentisate
-
 Chlamydomonas reinhardtii diphosphate + (3-geranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranyl diphosphate + homogentisate
-
 Arabidopsis thaliana diphosphate + (3-geranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranylgeranyl diphosphate + homogentisate
-
 Spinacia oleracea diphosphate + (3-geranylgeranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranylgeranyl diphosphate + homogentisate
-
 Chlamydomonas reinhardtii diphosphate + (3-geranylgeranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
geranylgeranyl diphosphate + homogentisate
-
 Arabidopsis thaliana diphosphate + (3-geranylgeranyl-2,5-dihydroxyphenyl)acetate no decarboxylation of product, 95% of the total prenylated reaction products formed are carboxylic acids ?
additional information enzyme uses not only solanesyl diphosphate but also short chain prenyl diphosphates of 10-20 carbon atoms as prenyl donors. With these donors, prenyl transfer is largely decoupled from decarboxylation, and thus the major products are 6-prenyl-1,4-benzoquinol-2-methylcarboxylates rather than 2-methyl-6-prenyl-1,4-benzoquinols. The 6-prenyl-1,4-benzoquinol-2-methylcarboxylates are not substrates for homogentisate prenyl transferase-catalyzed decarboxylation, and the enzyme kinetics associated with forming these products appears quite distinct from those for 2-methyl-6-prenyl-1,4-benzoquinol formation. A model for mechanism is as follows: prenyl diphosphate binds to homogentisate prenyl transferase to form at least two alternative complexes that go on to react differently with homogentisate and prenylate it either with or without it first being decarboxylated. It is supposed that solanesyl diphosphate binds tightly and preferentially in the mode that compels prenylation with decarboxylation Spinacia oleracea ?
-
 ?
additional information enzyme uses not only solanesyl diphosphate but also short chain prenyl diphosphates of 10-20 carbon atoms as prenyl donors. With these donors, prenyl transfer is largely decoupled from decarboxylation, and thus the major products are 6-prenyl-1,4-benzoquinol-2-methylcarboxylates rather than 2-methyl-6-prenyl-1,4-benzoquinols. The 6-prenyl-1,4-benzoquinol-2-methylcarboxylates are not substrates for homogentisate prenyl transferase-catalyzed decarboxylation, and the enzyme kinetics associated with forming these products appears quite distinct from those for 2-methyl-6-prenyl-1,4-benzoquinol formation. A model for mechanism is as follows: prenyl diphosphate binds to homogentisate prenyl transferase to form at least two alternative complexes that go on to react differently with homogentisate and prenylate it either with or without it first being decarboxylated. It is supposed that solanesyl diphosphate binds tightly and preferentially in the mode that compels prenylation with decarboxylation Chlamydomonas reinhardtii ?
-
 ?
additional information enzyme uses not only solanesyl diphosphate but also short chain prenyl diphosphates of 10-20 carbon atoms as prenyl donors. With these donors, prenyl transfer is largely decoupled from decarboxylation, and thus the major products are 6-prenyl-1,4-benzoquinol-2-methylcarboxylates rather than 2-methyl-6-prenyl-1,4-benzoquinols. The 6-prenyl-1,4-benzoquinol-2-methylcarboxylates are not substrates for homogentisate prenyl transferase-catalyzed decarboxylation, and the enzyme kinetics associated with forming these products appears quite distinct from those for 2-methyl-6-prenyl-1,4-benzoquinol formation. A model for mechanism is as follows: prenyl diphosphate binds to homogentisate prenyl transferase to form at least two alternative complexes that go on to react differently with homogentisate and prenylate it either with or without it first being decarboxylated. It is supposed that solanesyl diphosphate binds tightly and preferentially in the mode that compels prenylation with decarboxylation Arabidopsis thaliana ?
-
 ?
solanesyl diphosphate + homogentisate
-
 Spinacia oleracea diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
-
 ?
solanesyl diphosphate + homogentisate
-
 Chlamydomonas reinhardtii diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
-
 ?
solanesyl diphosphate + homogentisate
-
 Arabidopsis thaliana diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
-
 ?

Synonyms

Synonyms Comment Organism
At3g11945
-
 Arabidopsis thaliana
Hpt2
-
 Arabidopsis thaliana
VTE2
-
 Chlamydomonas reinhardtii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.038
-
 haloxydine pH 8.5, 28°C Chlamydomonas reinhardtii