Geranyl diphosphate

Geranyl diphosphate is a lipid of Prenol Lipids (PR) class. The involved functions are known as Prenylation, Anabolism, Biochemical Pathway and Methylation. Geranyl diphosphate often locates in Membrane and Plastids. The associated genes with Geranyl diphosphate are GGPS1 gene, NKS1 gene, COQ2 gene and MIB1 gene.

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Introduction

To understand associated biological information of Geranyl 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 Geranyl 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 Geranyl 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 Geranyl diphosphate?

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What functions are associated with Geranyl diphosphate?


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What lipids are associated with Geranyl diphosphate?

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

What genes are associated with Geranyl diphosphate?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Geranyl diphosphate?

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

NCBI Entrez Crosslinks

All references with Geranyl diphosphate

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Authors Title Published Journal PubMed Link
Zhang YL and Li ZX Functional analysis and molecular docking identify two active short-chain prenyltransferases in the green peach aphid, Myzus persicae. 2012 Arch. Insect Biochem. Physiol. pmid:22696503
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
Sillero MA et al. Synthesis of ATP derivatives of compounds of the mevalonate pathway (isopentenyl di- and triphosphate; geranyl di- and triphosphate, farnesyl di- and triphosphate, and dimethylallyl diphosphate) catalyzed by T4 RNA ligase, T4 DNA ligase and other ligases Potential relationship with the effect of bisphosphonates on osteoclasts. 2009 Biochem. Pharmacol. pmid:19414000
Micali E et al. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. 2001 Biochemistry pmid:11591144
Köksal M et al. Structure of geranyl diphosphate C-methyltransferase from Streptomyces coelicolor and implications for the mechanism of isoprenoid modification. 2012 Biochemistry pmid:22455498
Yang Y et al. Catalytic mechanism of aromatic prenylation by NphB. 2012 Biochemistry pmid:22385275
Barnard GF and Popják G Human liver prenyltransferase and its characterization. 1981 Biochim. Biophys. Acta pmid:7295734
Qiu Y and Li D Inhibition of mevalonate 5-diphosphate decarboxylase by fluorinated substrate analogs. 2006 Biochim. Biophys. Acta pmid:16626865
Tsuji F et al. The geranyl-modified tryptophan residue is crucial for ComXRO-E-2 pheromone biological activity. 2011 Bioorg. Med. Chem. Lett. pmid:21636272
Nagaki M et al. Substrate specificities of wild and mutated farnesyl diphosphate synthases from Bacillus stearothermophilus with artificial substrates. 2007 Biosci. Biotechnol. Biochem. pmid:17617711