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

Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.

The Journal of biological chemistry - 5 Apr 2002

Battaile Kevin P, Molin-Case JoAnn, Paschke Rosemary, Wang Ming, Bennett Dennis, Vockley Jerry, Kim Jung-Ja P

Abstract excerpt

The acyl-CoA dehydrogenases are a family of flavin adenine dinucleotide-containing enzymes that catalyze the first step in the beta-oxidation of fatty acids and catabolism of some amino acids. They exhibit high sequence identity and yet are quite specific in their substrate binding. Short chain acyl-CoA dehydrogenase has maximal activity toward butyryl-CoA and negligible activity toward substrates longer than...

Read the complete abstract on PubMed

Topics

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

Share to Acyl-CoA Dehydrogenase
Share to Acyl-CoA Dehydrogenases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Acyl Coenzyme A

Share to Crystallography, X-Ray

Share to DNA, Complementary

Share to Oxygen

Share to Protein Conformation

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 11812788
DOI: 10.1074/jbc.M111296200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.PMID 11812788Read ↗

Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases.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 ↗

Structure and Substrate Specificity of Human Short-Chain Acyl-CoA Dehydrogenase and Insights into Pathogenicity of Disease-Associated Mutations.Semantic proximity Read ↗

Crystal structure of rat carnitine palmitoyltransferase II (CPT-II).Semantic proximity Read ↗

Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.Semantic proximity Read ↗

Short-chain acyl-coenzyme A dehydrogenase deficiency.Semantic proximity Read ↗

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

The acyl-CoA dehydrogenase family: homology and divergence of primary sequence of four acyl-CoA dehydrogenases, and consideration of their functional significance.Semantic proximity Read ↗

Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.Semantic proximity Read ↗

Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.Semantic proximity Read ↗

Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency.Semantic proximity Read ↗

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli.Semantic proximity Read ↗

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