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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Chlamydomonas reinhardtii | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | Q1ACB3 | - |
- |
Chlamydomonas reinhardtii | A1JHN0 | - |
- |
Spinacia oleracea | - |
- |
- |
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 | Comment | Organism |
---|---|---|
At3g11945 | - |
Arabidopsis thaliana |
Hpt2 | - |
Arabidopsis thaliana |
VTE2 | - |
Chlamydomonas reinhardtii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.038 | - |
haloxydine | pH 8.5, 28°C | Chlamydomonas reinhardtii |