دورية أكاديمية
أعرض في EDS

Structural basis for expanded substrate specificities of human long chain acyl-CoA dehydrogenase and related acyl-CoA dehydrogenases.

التفاصيل البيبلوغرافية
العنوان: Structural basis for expanded substrate specificities of human long chain acyl-CoA dehydrogenase and related acyl-CoA dehydrogenases.
المؤلفون: Narayanan B; Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, 53226, USA., Xia C; Department of Chemistry and Biochemistry, College of Arts and Sciences, University of North Florida, Jacksonville, FL, 32224, USA., McAndrew R; Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, 53226, USA.; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA, 94740, USA., Shen AL; McArdle Laboratory for Cancer Research, Department of Oncology, University of Wisconsin-Madison, Madison, WI, 53706, USA., Kim JP; Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, 53226, USA. jjkim@mcw.edu.
المصدر: Scientific reports [Sci Rep] 2024 Jun 05; Vol. 14 (1), pp. 12976. Date of Electronic Publication: 2024 Jun 05.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London : Nature Publishing Group, copyright 2011-
مواضيع طبية MeSH: Acyl-CoA Dehydrogenase, Long-Chain*/metabolism , Acyl-CoA Dehydrogenase, Long-Chain*/genetics , Acyl-CoA Dehydrogenase, Long-Chain*/chemistry , Models, Molecular*, Substrate Specificity ; Humans ; Crystallography, X-Ray ; Catalytic Domain ; Acyl-CoA Dehydrogenases/metabolism ; Acyl-CoA Dehydrogenases/genetics ; Acyl-CoA Dehydrogenases/chemistry ; Protein Conformation ; Amino Acid Sequence
مستخلص: Crystal structures of human long-chain acyl-CoA dehydrogenase (LCAD) and the catalytically inactive Glu291Gln mutant, have been determined. These structures suggest that LCAD harbors functions beyond its historically defined role in mitochondrial β-oxidation of long and medium-chain fatty acids. LCAD is a homotetramer containing one FAD per 43 kDa subunit with Glu291 as the catalytic base. The substrate binding cavity of LCAD reveals key differences which makes it specific for longer and branched chain substrates. The presence of Pro132 near the start of the E helix leads to helix unwinding that, together with adjacent smaller residues, permits binding of bulky substrates such as 3α, 7α, l2α-trihydroxy-5β-cholestan-26-oyl-CoA. This structural element is also utilized by ACAD11, a eucaryotic ACAD of unknown function, as well as bacterial ACADs known to metabolize sterol substrates. Sequence comparison suggests that ACAD10, another ACAD of unknown function, may also share this substrate specificity. These results suggest that LCAD, ACAD10, ACAD11 constitute a distinct class of eucaryotic acyl CoA dehydrogenases.
(© 2024. The Author(s).)
التعليقات: Update of: Res Sq. 2024 Feb 29:rs.3.rs-3980524. doi: 10.21203/rs.3.rs-3980524/v1. (PMID: 38464032)
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معلومات مُعتمدة: R01 GM029076 United States GM NIGMS NIH HHS; R35-ES028377 United States NH NIH HHS; GM29076 United States NH NIH HHS
المشرفين على المادة: EC 1.3.8.8 (Acyl-CoA Dehydrogenase, Long-Chain)
EC 1.3.- (Acyl-CoA Dehydrogenases)
تواريخ الأحداث: Date Created: 20240605 Date Completed: 20240605 Latest Revision: 20240617
رمز التحديث: 20240617
مُعرف محوري في PubMed: PMC11153573
DOI: 10.1038/s41598-024-63027-6
PMID: 38839792
قاعدة البيانات: MEDLINE
الوصف
تدمد:2045-2322
DOI:10.1038/s41598-024-63027-6