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Literature summary for 2.5.1.1 extracted from

  • Chang, T.H.; Hsieh, F.L.; Ko, T.P.; Teng, K.H.; Liang, P.H.; Wang, A.H.
    Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation (2010), Plant Cell, 22, 454-467.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme forms a heterotetramer of two catalytic large plus two regulatory small subunits. No activity is detected for individually expressed large or small subunits Mentha x piperita

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mentha x piperita in vitro, but not in vivo, enzyme shows additional geranylgeranyl diphosphate synthase activity, EC 2.5.1.29 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mentha x piperita
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + isopentenyl diphosphate
-
 Mentha x piperita diphosphate + geranyl diphosphate
-
 ?
additional information in vitro, but not in vivo, enzyme shows additional geranylgeranyl diphosphate synthase activity, EC 2.5.1.29 Mentha x piperita ?
-
 ?

Subunits

Subunits Comment Organism
tetramer enzyme forms a heterotetramer of two catalytic large plus two regulatory small subunits, crystallization data. Mentha x piperita