EC number:5.4.99.64

Enzyme

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     5. Isomerases
        5.4 Intramolecular transferases
            5.4.99 Transferring other groups
ID:5.4.99.64
Description:2-hydroxyisobutanoyl-CoA mutase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.99.64
BRENDA Enzyme Link: BRENDA 5.4.99.64
KEGG Enzyme Link: KEGG5.4.99.64
BioCyc Enzyme Link: BioCyc 5.4.99.64
ExPASy Enzyme Link: ExPASy5.4.99.64
EC2PDB Enzyme Link: EC2PDB 5.4.99.64
ExplorEnz Enzyme Link: ExplorEnz 5.4.99.64
PRIAM enzyme-specific profiles Link: PRIAM 5.4.99.64
IntEnz Enzyme Link: IntEnz 5.4.99.64
MEDLINE Enzyme Link: MEDLINE 5.4.99.64

EC number:5.4.99.64

MSA:

5.4.99.64;
Phylogenetic Tree:

5.4.99.64;
Uniprot:
M-CSA:
RHEA:49592 2-hydroxyisobutanoyl-CoA = (3S)-hydroxybutanoyl-CoA
RULE(radius=1) [*:1]-[C;H0;+0:2](-[CH3;+0:3])(-[CH3;+0:4])-[OH;+0:5]>>[*:1]-[CH2;+0:2]-[CH;+0:4](-[CH3;+0:3])-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase.Kurteva-Yaneva N, Zahn M, Weichler MT, Starke R, Harms H, Müller RH, Sträter N, Rohwerder T2015 Apr 1025720495
Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA.Yaneva N, Schuster J, Schäfer F, Lede V, Przybylski D, Paproth T, Harms H, Müller RH, Rohwerder T2012 May 422433853