Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase.

Biochemical and biophysical research communications - 5 Dec 2008

Noike Motoyoshi, Ambo Takanori, Kikuchi Sayaka, Suzuki Toshihide, Yamashita Satoshi, Takahashi Seiji, Kurokawa Hirofumi, Mahapatra Sebabrata, Crick Dean C, Koyama Tanetoshi

Abstract excerpt

cis-Prenyltransferases catalyze the consecutive condensation of isopentenyl diphosphate (IPP) with allylic prenyl diphosphates, producing Z,E-mixed prenyl diphosphate. The Mycobacterium tuberculosis Z,E-farnesyl diphosphate synthase Rv1086 catalyzes the condensation of one molecule of IPP with geranyl diphosphate to yield Z,E-farnesyl diphosphate and is classified as a short-chain cis-prenyltransferase. To...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alkyl and Aryl Transferases
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Catalysis

Share to Conserved Sequence

Share to Leucine

Share to Mutagenesis, Insertional

Share to Mycobacterium tuberculosis

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 18790692
DOI: 10.1016/j.bbrc.2008.09.014
PMCID: PMC4747032

Genes

IPP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase.PMID 18790692Read ↗

An alternative mechanism of product chain-length determination in type III geranylgeranyl diphosphate synthase.Semantic proximity Read ↗

Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution.Semantic proximity Read ↗

The structural basis of chain length control in Rv1086.Semantic proximity Read ↗

Polyprenyl diphosphate synthases.Semantic proximity Read ↗

cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human DiseasesSemantic proximity Read ↗

Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction.Semantic proximity Read ↗

Structural basis for long-chain isoprenoids synthesis by <i>cis</i> -prenyltransferasesSemantic proximity Read ↗

Determination of residues responsible for substrate and product specificity of Solanum habrochaites short-chain cis-prenyltransferases.Semantic proximity Read ↗

The N-terminus and the chain-length determination domain play a role in the length of the isoprenoid product of the bifunctional Toxoplasma gondii farnesyl diphosphate synthase.Semantic proximity Read ↗

Structure-function studies of ultrahigh molecular weight isoprenes provide key insights into their biosynthesis.Semantic proximity Read ↗

Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations.Semantic proximity Read ↗

Connected cavity structure enables prenyl elongation across the dimer interface in mutated geranylfarnesyl diphosphate synthase from Methanosarcina mazei.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.