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

doi:10.1074/jbc.271.31.18831

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Article

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

The Journal of biological chemistry - 2 Aug 1996

Ohnuma S, Hirooka K, Hemmi H, Ishida C, Ohto C, Nishino T

Abstract excerpt

Prenyltransferases catalyze the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce prenyl diphosphates whose chain lengths are absolutely determined by each enzyme. To investigate the mechanism of the consecutive reaction and the determination of the ultimate...

Topics

Alcohols
Alkyl and Aryl Transferases
Amino Acid Sequence
Base Sequence
DNA Primers
DNA, Bacterial
Dimethylallyltranstransferase
Farnesyltranstransferase
Genes, Bacterial
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phenotype

Saccharomyces cerevisiae

Sequence Homology, Amino Acid

Substrate Specificity

Sulfolobus acidocaldarius

Transferases

Source

Open in PubMed

Identifiers

PMID: 8702542
DOI: 10.1074/jbc.271.31.18831

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8702542-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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