Literature summary for 2.5.1.30 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.

Search for more literature for 2.5.1.30

Cloned(Commentary)

Cloned (Comment)	Organism
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

Inhibitors	Comment	Organism	Structure
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]

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

Metals/Ions

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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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

Reaction	Comment	Organism	Reaction ID
(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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate	-	Bacillus subtilis	4 diphosphate + all-trans-heptaprenyl diphosphate	-	?
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	-	?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate	-	Bacillus subtilis	3 diphosphate + all-trans-heptaprenyl diphosphate	-	?
additional information	dimethylallyl diphosphate and geranyl diphosphate, are almost inactive as substrates	Bacillus subtilis	?	-	?

Subunits

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

Synonyms

Synonyms	Comment	Organism
HepPP synthase	-	Bacillus subtilis

pH Optimum

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)