The reduced stability of a plant alcohol dehydrogenase is due to the substitution of serine for a highly conserved phenylalanine residue.

doi:10.1007/BF00013750

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Article

The reduced stability of a plant alcohol dehydrogenase is due to the substitution of serine for a highly conserved phenylalanine residue.

Plant molecular biology - 1 Oct 1994

Garvin D F, Weeden N F, Doyle J J

Abstract excerpt

The zinc-binding long-chain alcohol dehydrogenases from plants and animals exhibit a considerable level of amino acid sequence conservation. While the functional importance of many of the conserved residues is known, the role of others has not yet been determined. We have identified a naturally o...

Topics

Alcohol Dehydrogenase
Alleles
Amino Acid Sequence
Animals
Base Sequence
Conserved Sequence
DNA Primers
DNA, Complementary
DNA, Plant
Electrophoresis, Starch Gel
Enzyme Stability
Fabaceae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Genes, Plant

Homozygote

Isoenzymes

Macromolecular Substances

Molecular Sequence Data

Phenylalanine

Source

Open in PubMed

Identifiers

PMID: 7948919
DOI: 10.1007/BF00013750

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7948919-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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