Discover Community Create You

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

Expression and purification of His-tagged rat mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase wild-type and Ser137 mutant proteins.

Protein expression and purification - 1 Oct 2004

Liu Xiaojun, Chu Xiusheng, Yu Wenhua, Li Pingfeng, Li Ding

Abstract excerpt

Mitochondrial 3-hydroxyacyl-CoA dehydrogenase is a key enzyme in the beta-oxidation of fatty acids. The deficiency of this enzyme in patients has been previously reported. We cloned the gene of rat mitochondrial 3-hydroxyacyl-CoA dehydrogenase in a bacterial expression vector pLM1 with six continuous histidine codons attached to the 5' of the gene. The cloned gene was overexpressed in Escherichia coli and the...

Read the complete abstract on PubMed

Topics

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

Share to 3-Hydroxyacyl CoA Dehydrogenases
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cysteine

Share to Models, Chemical

Share to Nickel

Share to Oxygen

Share to Serine

Share to Threonine

Source

Identifiers

PMID: 15358356
DOI: 10.1016/j.pep.2004.06.026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression and purification of His-tagged rat mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase wild-type and Ser137 mutant proteins.PMID 15358356Read ↗

Expression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins.Semantic proximity Read ↗

Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein.Semantic proximity Read ↗

Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations.Semantic proximity Read ↗

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

Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: a new method to identify the G1528C mutation in genomic DNA showing its high frequency (approximately 90%) and identification of a new mutation (T2198C).Semantic proximity Read ↗

Molecular cloning and nucleotide sequence of cDNAs encoding human short chain acyl-CoA dehydrogenase and study of the molecular basis of human short chain acyl-CoA dehydrogenase deficiency.Semantic proximity Read ↗

Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity.Semantic proximity Read ↗

Identification of the catalytic base in long chain acyl-CoA dehydrogenase.Semantic proximity Read ↗

Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria.Semantic proximity Read ↗

Mutation of Tyr375 to Lys375 allows medium-chain acyl-CoA dehydrogenase to acquire acyl-CoA oxidase activity.Semantic proximity Read ↗

Brassica juncea 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase 1: expression and characterization of recombinant wild-type and mutant enzymes.Semantic proximity Read ↗

Genetic reconstruction and characterization of the recombinant transacylase (E2b) component of bovine branched-chain alpha-keto acid dehydrogenase complex. Implication of histidine 391 as an active site residue.Semantic proximity Read ↗

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