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

Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.

ACS chemical biology - 18 Jun 2010

Dellas Nikki, Noel Joseph P

Abstract excerpt

The biosynthesis of isopentenyl diphosphate (IPP) from either the mevalonate (MVA) or the 1-deoxy-d-xylulose 5-phosphate (DXP) pathway provides the key metabolite for primary and secondary isoprenoid biosynthesis. Isoprenoid metabolism plays crucial roles in membrane stability, steroid biosynthesis, vitamin production, protein localization, defense and communication, photoprotection, sugar transport, and...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Crystallography, X-Ray
Share to Hemiterpenes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Organophosphorus Compounds

Share to Phosphorylation

Share to Polyisoprenyl Phosphates

Share to Protein Conformation

Share to Protein Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 20392112
DOI: 10.1021/cb1000313
PMCID: PMC2887675

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.PMID 20392112Read ↗

Molecular Basis for the Substrate Promiscuity of Isopentenyl Phosphate Kinase from Candidatus methanomethylophilus alvus.Semantic proximity Read ↗

Structural basis for nucleotide binding and reaction catalysis in mevalonate diphosphate decarboxylase.Semantic proximity Read ↗

The structure and catalytic cycle of a sodium-pumping pyrophosphatase.Semantic proximity Read ↗

The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis.Semantic proximity Read ↗

Expression and purification of Arg196 and Lys272 mutants of mevalonate kinase from Methanococcus jannaschii.Semantic proximity Read ↗

Extensive regulation of enzyme activity by phosphorylation in Escherichia coli.Semantic proximity Read ↗

Examining the role of intersubunit contacts in catalysis by 3-deoxy-d-manno-octulosonate 8-phosphate synthase.Semantic proximity Read ↗

Inorganic Polyphosphate: Essential for Growth and SurvivalSemantic proximity Read ↗

Functional evaluation of conserved basic residues in human phosphomevalonate kinase.Semantic proximity Read ↗

Mycoplasma pneumoniae HPr kinase/phosphorylase.Semantic proximity Read ↗

Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase.Semantic proximity Read ↗

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.Semantic proximity Read ↗

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