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

Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity.

Metabolic engineering - 1 Jan 2005

Lee Pyung Cheon, Petri Ralf, Mijts Benjamin N, Watts Kevin T, Schmidt-Dannert Claudia

Abstract excerpt

Directed evolution of farnesyl diphosphate (FPP, C15) synthase (IspA) of Escherichia coli was carried out by error-prone PCR with a color complementation screen utilizing C40 carotenoid pathway enzymes. This allowed IspA mutants with enhanced production of the C40 carotenoid precursor geranylgeranyl diphosphate (GGPP, C20) to be readily identified. Analysis of these mutants was carried out in order to better...

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 Carotenoids

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

Share to Computer Simulation

Share to Directed Molecular Evolution

Share to Escherichia coli

Share to Protein Engineering

Share to Sequence Analysis, Protein

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 15721807
DOI: 10.1016/j.ymben.2004.05.003

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

Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity.PMID 15721807Read ↗

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 ↗

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 ↗

Evolutionary analysis of the functional plasticity of Staphylococcus aureus C30 carotenoid synthase.Semantic proximity Read ↗

Characterization of a lysine-to-glutamic acid mutation in a conservative sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae.Semantic proximity Read ↗

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

The disruption of prenylation leads to pleiotropic rearrangements in cellular behavior in Staphylococcus aureus.Semantic proximity Read ↗

Evolution of the C30 carotenoid synthase CrtM for function in a C40 pathway.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 ↗

A T42M substitution in bacterial 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) generates enzymes with increased resistance to glyphosate.Semantic proximity Read ↗

Development of fatty acid-producing Corynebacterium glutamicum strains.Semantic proximity Read ↗

A subunit of decaprenyl diphosphate synthase stabilizes octaprenyl diphosphate synthase in Escherichia coli by forming a high-molecular weight complex.Semantic proximity Read ↗

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