Structural highlights
Function
HCMA_AQUTE Together with HcmB, catalyzes the isomerization of 2-hydroxyisobutyryl-CoA and 3-hydroxybutyryl-CoA. Is specific for 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA, and shows only very low activity with (R)-3-hydroxybutyryl-CoA, isobutyryl-CoA and butyryl-CoA (PubMed:22433853, PubMed:25720495). In vitro, can isomerize pivalyl-CoA and isovaleryl-CoA, with much lower efficiency (PubMed:25720495). Plays a central role in the degradation of substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites (PubMed:22433853).[1] [2]
References
- ↑ Yaneva N, Schuster J, Schäfer F, Lede V, Przybylski D, Paproth T, Harms H, Müller RH, Rohwerder T. Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA. J Biol Chem. 2012 May 4;287(19):15502-11. PMID:22433853 doi:10.1074/jbc.M111.314690
- ↑ Kurteva-Yaneva N, Zahn M, Weichler MT, Starke R, Harms H, Muller RH, Strater N, Rohwerder T. Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase. J Biol Chem. 2015 Apr 10;290(15):9727-37. doi: 10.1074/jbc.M115.645689. Epub 2015, Feb 26. PMID:25720495 doi:http://dx.doi.org/10.1074/jbc.M115.645689
