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

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

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?

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

What genes are associated with Neryl diphosphate?

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Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Neryl diphosphate?

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

NCBI Entrez Crosslinks

All references with Neryl diphosphate

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Authors Title Published Journal PubMed Link
Wise ML et al. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. 1998 J. Biol. Chem. pmid:9614092
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 et al. Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase. 1994 Arch. Biochem. Biophys. pmid:8117108
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
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
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
Appelkvist EL et al. Regulation of coenzyme Q biosynthesis. 1994 Mol. Aspects Med. pmid:7752843
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
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 and Felton M Conversion of [1-3H2,G-14C]geranyl pyrophosphate to cyclic monoterpenes without loss of tritium. 1981 Arch. Biochem. Biophys. pmid:7247415