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

Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations.

Biochemical and biophysical research communications - 11 Oct 2002

Hemmi Hisashi, Noike Motoyoshi, Nakayama Toru, Nishino Tokuzo

Abstract excerpt

The introduction of several sets of amino acid substitutions into the region around a substrate-binding site of a medium-chain (all-E) prenyl diphosphate synthase, hexaprenyl diphosphate synthase from a thermoacidophilic archaeon Sulfolobus solfataricus, to mimic the product determination mechanisms of various kinds of short-chain enzymes revealed that the structure around the region of the medium-chain enzyme...

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 Chromatography, Thin Layer

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

Share to Dimerization

Share to Mutagenesis, Site-Directed

Share to Plasmids

Share to Substrate Specificity

Share to Sulfolobus

Share to Temperature

Source

Identifiers

PMID: 12372398
DOI: 10.1016/s0006-291x(02)02348-3

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

Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations.PMID 12372398Read ↗

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

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

Polyprenyl diphosphate synthases.Semantic proximity Read ↗

Recognition of allylic substrates in Sulfolobus acidocaldarius geranylgeranyl diphosphate synthase: analysis using mutated enzymes and artificial allylic substrates.Semantic proximity Read ↗

Structural features conferring dual geranyl/farnesyl diphosphate synthase activity to an aphid prenyltransferase.Semantic proximity Read ↗

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

Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Semantic proximity Read ↗

Kinetic basis of sugar selection by a Y-family DNA polymerase from Sulfolobus solfataricus P2.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 ↗

Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling.Semantic proximity Read ↗

Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox.Semantic proximity Read ↗

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