Literature summary for 2.5.1.10 extracted from

Narita, K.; Ohnuma, S.I.; Nishino, T.
Protein design of geranyl diphosphate synthase. Structural features that define the product specificities of prenyltransferases (1999), J. Biochem., 126, 566-571.

Search for more literature for 2.5.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type, S82F, S82Y, S82W, L83F, L83Y, I84F and I84Y mutant enzymes in Escherichia coli	Geobacillus stearothermophilus

Protein Variants

Protein Variants	Comment	Organism
I84F	7.2% of wild-type activity with dimethylallyl diphosphate	Geobacillus stearothermophilus
I84Y	similiar activity as wild-type	Geobacillus stearothermophilus
L83F	similiar activity as wild-type	Geobacillus stearothermophilus
L83Y	similiar activity as wild-type	Geobacillus stearothermophilus
S82F	produces exclusively geranyl diphosphate, i.e. the mutant enzyme has changed from a farnesyl diphosphate synthase to a geranyl diphosphate synthase	Geobacillus stearothermophilus
S82W	no prenyl transferase activity	Geobacillus stearothermophilus
S82Y	similiar activity as wild-type	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dimethylallyl diphosphate + 2 isopentenyl diphosphate	no activity with farnesyl diphosphate	Geobacillus stearothermophilus	(E,E)-farnesyl diphosphate + 2 diphosphate	-	?

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Release 2023.1 (January 2023)