Literature summary for 2.5.1.10 extracted from

Park, J.; Rodionov, D.; De Schutter, J.W.; Lin, Y.S.; Tsantrizos, Y.S.; Berghuis, A.M.
Crystallographic and thermodynamic characterization of phenylaminopyridine bisphosphonates binding to human farnesyl pyrophosphate synthase (2017), PLoS ONE, 12, e0186447 .

Search for more literature for 2.5.1.10

Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion in sitting drops. In order to examine the actual binding interactions between the new PNP-BPs and hFPPS, co-crystal structures with the key inhibitors YS05035, JDS05119, and JDS05120 are determined	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
JDS05119	-	Homo sapiens
JDS05120	-	Homo sapiens
risedronate	-	Homo sapiens
YS04070	-	Homo sapiens
YS05035	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
geranyl diphosphate + isopentenyl diphosphate	Homo sapiens	-	diphosphate + (2E,6E)-farnesyl diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14324	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
geranyl diphosphate + isopentenyl diphosphate	-	Homo sapiens	diphosphate + (2E,6E)-farnesyl diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
farnesyl pyrophosphate synthase	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme is a key regulator of the mevalonate pathway	Homo sapiens

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Release 2023.1 (January 2023)