ArticleThe Journal of biological chemistry2015
Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- The Expanding Reactivity of Cobamide-Containing Proteins: From Mechanistic Understanding to Non-native Biocatalysis.ACS catalysis · 2026Article
- Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for BNature communications · 2023Article
- Article
- Gut Microbiota Functional Traits, Blood pH, and Anti-GAD Antibodies Concur in the Clinical Characterization of T1D at Onset.International journal of molecular sciences · 2022Article
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (International ed. in English) · 2022Article
- Redox-Linked Coordination Chemistry Directs Vitamin BAccounts of chemical research · 2021Article
- Identification of lysine isobutyrylation as a new histone modification mark.Nucleic acids research · 2021Article
- New perspectives on butyrate assimilation in Rhodospirillum rubrum S1H under photoheterotrophic conditions.BMC microbiology · 2020Article
- Allosteric Regulation of Oligomerization by a BCell chemical biology · 2019Article
- Switch I-dependent allosteric signaling in a G-protein chaperone-BThe Journal of biological chemistry · 2017Article
- Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical BThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Acyl-CoA mutases are a growing class of adenosylcobalamin-dependent radical enzymes that perform challenging carbon skeleton rearrangements in primary and secondary metabolism. Members of this class of enzymes must precisely control substrate positioning to prevent oxidative interception of radical intermediates during catalysis. Our understanding of substrate specificity and catalysis in acyl-CoA mutases, however, is incomplete. Here, we present crystal structures of IcmF, a natural fusion protein variant of isobutyryl-CoA mutase, in complex with the adenosylcobalamin cofactor and four different acyl-CoA substrates. These structures demonstrate how the active site is designed to accommodate the aliphatic acyl chains of each substrate. The structures suggest that a conformational change of the 5'-deoxyadenosyl group from C2'-endo to C3'-endo could contribute to initiation of catalysis. Furthermore, detailed bioinformatic analyses guided by our structural findings identify critical determinants of acyl-CoA mutase substrate specificity and predict new acyl-CoA mutase-catalyzed reactions. These results expand our understanding of the substrate specificity and the catalytic scope of acyl-CoA mutases and could benefit engineering efforts for biotechnological applications ranging from production of biofuels and commercial products to hydrocarbon remediation.
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