Literature summary for 2.5.1.30 extracted from

Koike-Takeshita, A.; Koyama, T.; Ogura, K.
Intersubunit structure within heterodimers of medium-chain prenyl diphosphate synthases. Formation of a hybrid-type heptaprenyl diphosphate synthase (1998), J. Biochem., 124, 790-797.

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Protein Variants

Protein Variants	Comment	Organism
additional information	the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	P55784 and P55785	P55784: subunit 1, P55785: subunit 2	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate	-	Geobacillus stearothermophilus	4 diphosphate + all-trans-heptaprenyl diphosphate	-	?

Subunits

Subunits	Comment	Organism
More	the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases	Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)