Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation.

doi:10.1016/0925-4439(93)90068-c

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Article

Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation.

Biochimica et biophysica acta - 20 Oct 1993

Bross P, Andresen B S, Winter V, Kräutle F, Jensen T G, Nandy A, Kølvraa S, Ghisla S, Bolund L, Gregersen N

Abstract excerpt

The influence of co-overexpression of the bacterial chaperonins GroEL and GroES on solubility, tetramer formation and enzyme activity of three variants of heterologously-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) was analysed in order to investigate the molecular mechanism underly...

Topics

Acyl-CoA Dehydrogenase
Acyl-CoA Dehydrogenases
Bacterial Proteins
Base Sequence
Chaperonins
Escherichia coli
Gene Expression
Glutamates
Glutamic Acid
Glutamine
Humans
Lysine
Molecular Sequence Data

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Mutation

Plasmids

Protein Folding

Proteins

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Identifiers

PMID: 8104486
DOI: 10.1016/0925-4439(93)90068-c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8104486-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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