Literature summary for 2.5.1.90 extracted from

Zhang, J.; Zhang, X.; Zhang, R.; Wu, C.; Guo, Y.; Mao, X.; Guo, G.; Zhang, Y.; Wang, D.C.; Li, D.; Zou, Q.
Modeling studies with Helicobacter pylori octaprenyl pyrophosphate synthase reveal the enzymatic mechanism of trans-prenyltransferases (2012), Int. J. Biochem. Cell Biol., 44, 2116-2123.

Crystallization (Commentary)

Crystallization (Comment)	Organism
native enzyme and selenomethionine derivative, to 2.0 A and 2.8 A resolution, respectively. Residues Arg87, Lys36 and Arg39 are essential for isopentenyl diphosphate binding. Residues Lys162, Lys224 and Gln197 are involved in farnesyl diphosphate binding. The second DDXXD motif may be involved in farnesyl diphosphate binding by Mg2+-mediated interactions, Leu127 is probably involved in product chain length determination and the intermediate products such as geranylgeranyl diphosphate need a rearrange to occupy the binding site of farnesyl diphosphate and then isopentenyl diphosphate is reloaded	Helicobacter pylori

Crystallization (Comment)

Organism

native enzyme and selenomethionine derivative, to 2.0 A and 2.8 A resolution, respectively. Residues Arg87, Lys36 and Arg39 are essential for isopentenyl diphosphate binding. Residues Lys162, Lys224 and Gln197 are involved in farnesyl diphosphate binding. The second DDXXD motif may be involved in farnesyl diphosphate binding by Mg2+-mediated interactions, Leu127 is probably involved in product chain length determination and the intermediate products such as geranylgeranyl diphosphate need a rearrange to occupy the binding site of farnesyl diphosphate and then isopentenyl diphosphate is reloaded

Helicobacter pylori

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	O25023	-	-

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Release 2023.1 (January 2023)