Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.

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Article

Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.

The Journal of biological chemistry - 5 May 1990

Bross P, Engst S, Strauss A W, Kelly D P, Rasched I, Ghisla S

Abstract excerpt

The cDNA of human medium chain acyl-CoA dehydrogenase (MCADH) was modified by in vitro mutagenesis, and the sequence encoding the mature form of MCADH was introduced into an inducible expression plasmid. We observed synthesis of the protein in Escherichia coli cells transformed with this plasmid with measurable MCADH enzyme activity in cell extracts. Glutamic acid 376, which has been proposed by Powell and Thorpe...

Topics

Acyl-CoA Dehydrogenase
Acyl-CoA Dehydrogenases
Animals
Base Sequence
Binding Sites
Cloning, Molecular
Escherichia coli
Glutamates
Glutamic Acid
Glutamine
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kidney

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Recombinant Proteins

Restriction Mapping

Spectrophotometry

Source

Open in PubMed

Identifiers

PMID: 1970566

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1970566-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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