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Literature summary extracted from

  • Zhang, Y.W.; Koyama, T.; Marecak, D.M.; Prestwich, G.D.; Maki, Y.; Ogura, K.
    Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex (1998), Biochemistry, 37, 13411-13420.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.30 to explore the dynamic interaction of the two dissociable components during catalysis, expression vector systems for the two structural genes, gerC1 and gerC3, are constructed separately, and the two components are overproduced in Escherichia coli cells Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.30 additional information enzymatic activity is inhibited by each antiserum against component I or component II, indicating that either component I or component II is confirmed immunochemically to be essential for enzymatic activity Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.30 0.0071
-
 (2E,6E)-farnesyl diphosphate pH 8.5, 30°C Bacillus subtilis
2.5.1.30 0.0085
-
 geranylgeranyl diphosphate pH 8.5, 30°C Bacillus subtilis
2.5.1.30 0.0167
-
 isopentenyl diphosphate pH 8.5, 30°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.30 Mg2+ requires a divalent cation for the enzymatic activity with an optimal level of 1 mM Mg2+ or 2 mM Mn2+, respectively Bacillus subtilis
2.5.1.30 Mn2+ requires a divalent cation for the enzymatic activity with an optimal level of 1 mM Mg2+ or 2 mM Mn2+, respectively Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.30 29000
-
 1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE Bacillus subtilis
2.5.1.30 36000
-
 1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.30 (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate Bacillus subtilis
-
 4 diphosphate + all-trans-heptaprenyl diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.30 Bacillus subtilis P31112 and P31114 P31112: subunit 1, P31114: subunit 2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.30 to explore the dynamic interaction of the two dissociable components during catalysis, expression vector systems for the two structural genes, gerC1 and gerC3, are constructed separately, and the two components are overproduced in Escherichia coli cells. Each component is purified homogeneously Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.30 (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate enzyme component I, enzyme component II, and farnesyl diphosphate-Mg2+ form a ternary complex during catalysis and that neither isopentenyl diphosphate nor the product, heptaprenyl diphosphate, is included in this complex, which probably represents a catalytically active state of the HepPP synthase. Component I is involved in allylic substrate recognition Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.30 (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
-
 Bacillus subtilis 4 diphosphate + all-trans-heptaprenyl diphosphate
-
 ?
2.5.1.30 all-trans-farnesyl diphosphate + 4 isopentenyl diphosphate enzyme component I, enzyme component II, and farnesyl diphosphate-Mg2+ form a ternary complex during catalysis and that neither isopentenyl diphosphate nor the product, heptaprenyl diphosphate, is included in this complex, which probably represents a catalytically active state of the HepPP synthase. Enzyme component I is involved in allylic substrate recognition Bacillus subtilis 4 diphosphate + all-trans-heptaprenyl diphosphate
-
 ?
2.5.1.30 geranylgeranyl diphosphate + 3 isopentenyl diphosphate
-
 Bacillus subtilis 3 diphosphate + all-trans-heptaprenyl diphosphate
-
 ?
2.5.1.30 additional information dimethylallyl diphosphate and geranyl diphosphate, are almost inactive as substrates Bacillus subtilis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.30 dimer 1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
2.5.1.30 HepPP synthase
-
 Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.30 7.5 9 recombinant enzyme Bacillus subtilis