Neryl diphosphate

Neryl diphosphate is a lipid of Prenol Lipids (PR) class. The involved functions are known as Phenomenon. Neryl diphosphate often locates in Chloroplasts and Head. The associated genes with Neryl diphosphate are IPP gene.

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Introduction

To understand associated biological information of Neryl diphosphate, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Neryl diphosphate?

There are no associated biomedical information in the current reference collection.

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with Neryl diphosphate

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PubChem Biomolecular Interactions and Pathways

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What cellular locations are associated with Neryl diphosphate?

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What functions are associated with Neryl diphosphate?


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What lipids are associated with Neryl diphosphate?

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What genes are associated with Neryl diphosphate?

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What common seen animal models are associated with Neryl diphosphate?

There are no associated biomedical information in the current reference collection.

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All references with Neryl diphosphate

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Authors Title Published Journal PubMed Link
Croteau RB et al. Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates. 1985 Biochemistry pmid:4084562
Cane DE Cell-free studies of monoterpene and sesquiterpene biosynthesis. 1983 Biochem. Soc. Trans. pmid:6642060
Räikkönen J et al. Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells. 2010 Biochem. Pharmacol. pmid:19819230
Chen AP et al. Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase. 2005 Biochem. J. pmid:15447632
Glickman JF and Schmid A Farnesyl pyrophosphate synthase: real-time kinetics and inhibition by nitrogen-containing bisphosphonates in a scintillation assay. 2007 Assay Drug Dev Technol pmid:17477829
Lewinsohn E et al. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. 1992 Arch. Biochem. Biophys. pmid:1731633
Wheeler CJ et al. Uncompetitive inhibition of monoterpene cyclases by an analog of the substrate geranyl pyrophosphate and inhibition of monoterpene biosynthesis in vivo by an analog of geraniol. 1990 Arch. Biochem. Biophys. pmid:2350172
Croteau R et al. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. 1990 Arch. Biochem. Biophys. pmid:2178556
Hallahan TW and Croteau R Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate. 1989 Arch. Biochem. Biophys. pmid:2916845
Hallahan TW and Croteau R Monoterpene biosynthesis: demonstration of a geranyl pyrophosphate:sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis). 1988 Arch. Biochem. Biophys. pmid:3401015
Ness GC et al. Influence of mevalonate kinase on studies of the MgATP-dependent inactivator of 3-hydroxy-3-methylglutaryl coenzyme A reductase. 1982 Arch. Biochem. Biophys. pmid:6284035
Croteau R et al. Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase. 1994 Arch. Biochem. Biophys. pmid:8117108
LaFever RE and Croteau R Hydride shifts in the biosynthesis of the p-menthane monoterpenes alpha-terpinene, gamma-terpinene, and beta-phellandrene. 1993 Arch. Biochem. Biophys. pmid:8460944
Croteau R and Felton M Conversion of [1-3H2,G-14C]geranyl pyrophosphate to cyclic monoterpenes without loss of tritium. 1981 Arch. Biochem. Biophys. pmid:7247415
Croteau R et al. Biosynthesis of monoterpenes: conversion of the acyclic precursors geranyl pyrophosphate and neryl pyrophosphate to the rearranged monoterpenes fenchol and fenchone by a soluble enzyme preparation from fennel (Foeniculum vulgare). 1980 Arch. Biochem. Biophys. pmid:7436420
Croteau R et al. Biosynthesis of monoterpenes: preliminary characterization of i-endo-fenchol synthetase from fennel (Foeniculum vulgare) and evidence that no free intermediate is involved in the cyclization of geranyl pyrophosphate to the rearranged product. 1980 Arch. Biochem. Biophys. pmid:7436421
Pichersky E et al. Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri. 1995 Arch. Biochem. Biophys. pmid:7864636
Wagschal KC et al. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). 1994 Arch. Biochem. Biophys. pmid:8109978
Pyun HJ et al. Stereochemistry of the proton elimination in the formation of (+)- and (-)-alpha-pinene by monoterpene cyclases from sage (Salvia officinalis). 1994 Arch. Biochem. Biophys. pmid:8109979
Kjonaas R and Croteau R Demonstration that limonene is the first cyclic intermediate in the biosynthesis of oxygenated p-menthane monoterpenes in Mentha piperita and other Mentha species. 1983 Arch. Biochem. Biophys. pmid:6830247