EC
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5.3.3.20
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Transferred entry: | 2-hydroxyisobutanoyl-CoA mutase. Now EC 5.4.99.64, 2-hydroxyisobutanoyl-CoA mutase
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[EC 5.3.3.20 created 2016, deleted 2017] |
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EC |
5.4.99.64 |
Accepted name: |
2-hydroxyisobutanoyl-CoA mutase |
Reaction: |
2-hydroxy-2-methylpropanoyl-CoA = (S)-3-hydroxybutanoyl-CoA |
Glossary: |
2-hydroxy-2-methylpropanoyl-CoA = 2-hydroxyisobutanoyl-CoA |
Other name(s): |
hcmAB (gene names) |
Systematic name: |
2-hydroxy-2-methylpropanoyl-CoA mutase |
Comments: |
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yaneva, N., Schuster, J., Schafer, F., Lede, V., Przybylski, D., Paproth, T., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA. J. Biol. Chem. 287 (2012) 15502–15511. [DOI] [PMID: 22433853] |
2. |
Kurteva-Yaneva, N., Zahn, M., Weichler, M.T., Starke, R., Harms, H., Muller, R.H., Strater, N. and Rohwerder, T. Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase. J. Biol. Chem. 290 (2015) 9727–9737. [DOI] [PMID: 25720495] |
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[EC 5.4.99.64 created 2016 as EC 5.3.3.20, transferred 2017 to EC 5.4.99.64] |
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