ArticleThe Journal of biological chemistry2012
Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 40 citations in OpenAlex.
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- Aerobic catabolism of isobutylene byApplied and environmental microbiology · 2026Article
- Biodegradation of Poly(ε-caprolactone): Microorganisms, Enzymes, and Mechanisms.International journal of molecular sciences · 2025Review
- Exploring the Evolution-Coupling Hypothesis: Do Enzymes' Performance Gains Correlate with Increased Dissipation?Entropy (Basel, Switzerland) · 2025Article
- New-to-nature CONature communications · 2024Article
- Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for BNature communications · 2023Article
- A Review of the Biotechnological Production of Methacrylic Acid.Frontiers in bioengineering and biotechnology · 2020Review
- Actinobacterial Degradation of 2-Hydroxyisobutyric Acid Proceeds via Acetone and Formyl-CoA by Employing a Thiamine-Dependent Lyase Reaction.Frontiers in microbiology · 2020Article
- Cofactor Selectivity in Methylmalonyl Coenzyme A Mutase, a Model Cobamide-Dependent Enzyme.mBio · 2019Article
- Production of 2-Hydroxyisobutyric Acid from Methanol by Methylobacterium extorquens AM1 Expressing (R)-3-Hydroxybutyryl Coenzyme A-Isomerizing Enzymes.Applied and environmental microbiology · 2017Article
- Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.The Journal of biological chemistry · 2015Article
- Engineered and Native Coenzyme B12-dependent Isovaleryl-CoA/Pivalyl-CoA Mutase.The Journal of biological chemistry · 2015Article
- Thermophilic Coenzyme B12-Dependent Acyl Coenzyme A (CoA) Mutase from Kyrpidia tusciae DSM 2912 Preferentially Catalyzes Isomerization of (R)-3-Hydroxybutyryl-CoA and 2-Hydroxyisobutyryl-CoA.Applied and environmental microbiology · 2015Article
- Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase.The Journal of biological chemistry · 2015Article
- Metabolism of 2-methylpropene (isobutylene) by the aerobic bacterium Mycobacterium sp. strain ELW1.Applied and environmental microbiology · 2015Article
- The anaerobic degradation of gaseous, nonmethane alkanes - From in situ processes to microorganisms.Computational and structural biotechnology journal · 2015Review
- The undernourished neonatal mouse metabolome reveals evidence of liver and biliary dysfunction, inflammation, and oxidative stress.The Journal of nutrition · 2014Article
- Constitutive expression of the cytochrome P450 EthABCD monooxygenase system enables degradation of synthetic dialkyl ethers in Aquincola tertiaricarbonis L108.Applied and environmental microbiology · 2013Article
- Novel B(12)-dependent acyl-CoA mutases and their biotechnological potential.Biochemistry · 2012Review
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9 authors at 1 institution in 1 country.
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Abstract
Coenzyme B(12)-dependent acyl-CoA mutases are radical enzymes catalyzing reversible carbon skeleton rearrangements in carboxylic acids. Here, we describe 2-hydroxyisobutyryl-CoA mutase (HCM) found in the bacterium Aquincola tertiaricarbonis as a novel member of the mutase family. HCM specifically catalyzes the interconversion of 2-hydroxyisobutyryl- and (S)-3-hydroxybutyryl-CoA. Like isobutyryl-CoA mutase, HCM consists of a large substrate- and a small B(12)-binding subunit, HcmA and HcmB, respectively. However, it is thus far the only acyl-CoA mutase showing substrate specificity for hydroxylated carboxylic acids. Complete loss of 2-hydroxyisobutyric acid degradation capacity in hcmA and hcmB knock-out mutants established the central role of HCM in A. tertiaricarbonis for degrading substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites. Sequence analysis revealed several HCM-like enzymes in other bacterial strains not related to MTBE degradation, indicating that HCM may also be involved in other pathways. In all strains, hcmA and hcmB are associated with genes encoding for a putative acyl-CoA synthetase and a MeaB-like chaperone. Activity and substrate specificity of wild-type enzyme and active site mutants HcmA I90V, I90F, and I90Y clearly demonstrated that HCM belongs to a new subfamily of B(12)-dependent acyl-CoA mutases.
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