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• W2152704187 endingPage "467" @default.
• W2152704187 startingPage "454" @default.
• W2152704187 abstract "Abstract Terpenes (isoprenoids), derived from isoprenyl pyrophosphates, are versatile natural compounds that act as metabolism mediators, plant volatiles, and ecological communicators. Divergent evolution of homomeric prenyltransferases (PTSs) has allowed PTSs to optimize their active-site pockets to achieve catalytic fidelity and diversity. Little is known about heteromeric PTSs, particularly the mechanisms regulating formation of specific products. Here, we report the crystal structure of the (LSU · SSU)2-type (LSU/SSU = large/small subunit) heterotetrameric geranyl pyrophosphate synthase (GPPS) from mint (Mentha piperita). The LSU and SSU of mint GPPS are responsible for catalysis and regulation, respectively, and this SSU lacks the essential catalytic amino acid residues found in LSU and other PTSs. Whereas no activity was detected for individually expressed LSU or SSU, the intact (LSU · SSU)2 tetramer produced not only C10-GPP at the beginning of the reaction but also C20-GGPP (geranylgeranyl pyrophosphate) at longer reaction times. The activity for synthesizing C10-GPP and C20-GGPP, but not C15-farnesyl pyrophosphate, reflects a conserved active-site structure of the LSU and the closely related mustard (Sinapis alba) homodimeric GGPPS. Furthermore, using a genetic complementation system, we showed that no C20-GGPP is produced by the mint GPPS in vivo. Presumably through protein–protein interactions, the SSU remodels the active-site cavity of LSU for synthesizing C10-GPP, the precursor of volatile C10-monoterpenes." @default.
• W2152704187 created "2016-06-24" @default.
• W2152704187 creator A5006129823 @default.
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• W2152704187 creator A5065052234 @default.
• W2152704187 creator A5065536494 @default.
• W2152704187 creator A5076281538 @default.
• W2152704187 date "2010-02-01" @default.
• W2152704187 modified "2023-10-06" @default.
• W2152704187 title "Structure of a Heterotetrameric Geranyl Pyrophosphate Synthase from Mint (<i>Mentha piperita</i>) Reveals Intersubunit Regulation " @default.
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• W2152704187 doi "https://doi.org/10.1105/tpc.109.071738" @default.
• W2152704187 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2845413" @default.
• W2152704187 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20139160" @default.
• W2152704187 hasPublicationYear "2010" @default.
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