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Literature summary extracted from

  • Maheshwari, S.; Kim, Y.S.; Aripirala, S.; Murphy, M.; Amzel, L.M.; Gabelli, S.B.
    Identifying structural determinants of product specificity in Leishmania major farnesyl diphosphate synthase (2020), Biochemistry, 59, 2751-2759 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.10 expression in Escherichia coli BL21 (DE3) cells Leishmania major

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.10 crystals of mutant enzymes E97Y, T164Y, and T164W, are produced using the hanging drop vapor diffusion technique at 18°C. Proteins are co-crystallized with inhibitor 476A and substrate IPP in the presence of MgCl Leishmania major
2.5.1.10 hanging drop vapor diffusion technique at 18°C. Crystal structures of mutant enzymes E97Y, T164W, and T164Y bound with 3-butyl-1-(2,2-diphosphonoethyl)pyridinium, isopentenyl diphosphate, and modeled farnesyl diphosphate provide strong evidence that these mutations produce the observed effects by altering the size of the binding pocket for the growing isoprenoid chain in the active site of the enzyme Leishmania major

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.10 T164F mutation completely abolishes the activity Leishmania major
2.5.1.10 T164F mutation completely abolishes the activity of the enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme Leishmania major
2.5.1.10 T164W mutation completely abolishes the activity Leishmania major
2.5.1.10 T164W mutation completely abolishes the activity of the enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme Leishmania major
2.5.1.10 T164Y mutation displays dual product specificity and produces a mixture geranyl diphosphate and farnesyl diphosphate as final products, with an activity for farnesyl diphosphate synthesis that is lower than that of the wild-type enzyme Leishmania major
2.5.1.10 T164Y mutation displays dual product specificity and produces a mixture geranyl diphosphate and farnesyl diphosphate as final products, with an activity for farnesyl diphosphate synthesis that is lower than that of the wild-type enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme Leishmania major

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.10 3-butyl-1-(2,2-diphosphonoethyl)pyridinium
-
 Leishmania major

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.10 dimethylallyl diphosphate + isopentenyl diphosphate Leishmania major the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate which is a precursor for the biosynthesis of a vast majority of isoprenoids diphosphate + geranyl diphosphate
-
 ?
2.5.1.10 dimethylallyl diphosphate + isopentenyl diphosphate Leishmania major the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate with isopentenyl diphosphate and the resulting geranyl diphosphate with another molecule of isopentenyl diphosphate, eventually producing farnesyl diphosphate diphosphate + geranyl diphosphate
-
 ?
2.5.1.10 geranyl diphosphate + isopentenyl diphosphate Leishmania major the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate which is a precursor for the biosynthesis of a vast majority of isoprenoids diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?
2.5.1.10 geranyl diphosphate + isopentenyl diphosphate Leishmania major the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate with isopentenyl diphosphate and the resulting geranyl diphosphate with another molecule of isopentenyl diphosphate, eventually producing farnesyl diphosphate diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.10 Leishmania major Q4QBL1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.10
-
 Leishmania major

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.10 dimethylallyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate which is a precursor for the biosynthesis of a vast majority of isoprenoids Leishmania major diphosphate + geranyl diphosphate
-
 ?
2.5.1.10 dimethylallyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate with isopentenyl diphosphate and the resulting geranyl diphosphate with another molecule of isopentenyl diphosphate, eventually producing farnesyl diphosphate Leishmania major diphosphate + geranyl diphosphate
-
 ?
2.5.1.10 dimethylallyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate Leishmania major diphosphate + geranyl diphosphate
-
 ?
2.5.1.10 geranyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate which is a precursor for the biosynthesis of a vast majority of isoprenoids Leishmania major diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?
2.5.1.10 geranyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate with isopentenyl diphosphate and the resulting geranyl diphosphate with another molecule of isopentenyl diphosphate, eventually producing farnesyl diphosphate Leishmania major diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?
2.5.1.10 geranyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP) and the resulting geranyl diphosphate (GPP) with another molecule of IPP, eventually producing farnesyl diphosphate Leishmania major diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.10 homodimer
-
 Leishmania major

Synonyms

EC Number Synonyms Comment Organism
2.5.1.10 farnesyl diphosphate synthase
-
 Leishmania major
2.5.1.10 FPPS
-
 Leishmania major

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.10 94
-
 Tm-value above, wild-type and mutant enzymes Leishmania major

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.10 8
-
-
 Leishmania major

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.5.1.10 7.5 8 most stable from pH 7.5 to 8.0 Leishmania major