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

The multifunctional isopropyl alcohol dehydrogenase of Phytomonas sp. could be the result of a horizontal gene transfer from a bacterium to the trypanosomatid lineage.

The Journal of biological chemistry - 19 Sept 2003

Molinas Sara M, Altabe Silvia G, Opperdoes Fred R, Rider Mark H, Michels Paul A M, Uttaro Antonio D

Abstract excerpt

Isopropyl alcohol dehydrogenase (iPDH) is a dimeric mitochondrial alcohol dehydrogenase (ADH), so far detected within the Trypanosomatidae only in the genus Phytomonas. The cloning, sequencing, and heterologous expression of the two gene alleles of the enzyme revealed that it is a zinc-dependent...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Dehydrogenase
Share to Blotting, Southern
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gas Chromatography-Mass Spectrometry

Share to Gene Transfer, Horizontal

Share to Protein Isoforms

Share to Trypanosoma

Source

Identifiers

PMID: 12853449
DOI: 10.1074/jbc.M305666200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12853449-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The multifunctional isopropyl alcohol dehydrogenase of Phytomonas sp. could be the result of a horizontal gene transfer from a bacterium to the trypanosomatid lineage.PMID 12853449Read ↗

A unique homodimeric NAD⁺-linked isocitrate dehydrogenase from the smallest autotrophic eukaryote Ostreococcus tauri.Semantic proximity Read ↗

Functional characterization of Arabidopsis thaliana isopropylmalate dehydrogenases reveals their important roles in gametophyte development.Semantic proximity Read ↗

Biosynthesis of Vitamins and Cofactors in Bacterium-Harbouring Trypanosomatids Depends on the Symbiotic Association as Revealed by Genomic AnalysesSemantic proximity Read ↗

Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilitiesSemantic proximity Read ↗

Multiple roles of proline transport and metabolism in trypanosomatidsSemantic proximity Read ↗

Isolation and molecular characterization of the shikimate dehydrogenase domain from the Toxoplasma gondii AROM complex.Semantic proximity Read ↗

Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed evolution.Semantic proximity Read ↗

A metabolic switch is involved in lifestyle decisions in Photorhabdus luminescens.Semantic proximity Read ↗

Phylogenetic and functional diversity of aldehyde-alcohol dehydrogenases in microalgae.Semantic proximity Read ↗

Isolation and characterization of a soluble and thermostable phosphite dehydrogenase from Ralstonia sp. strain 4506.Semantic proximity Read ↗

Investigating a catalytic mechanism of hyperthermophilic L-threonine dehydrogenase from Pyrococcus horikoshii.Semantic proximity Read ↗

Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108.Semantic proximity Read ↗

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