EC 2.8.3.21 - L-carnitine CoA-transferase

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IntEnz Enzyme Nomenclature
EC 2.8.3.21

Names

Accepted name:
L-carnitine CoA-transferase
Other names:
CaiB
crotonobetainyl/γ-butyrobetainyl-CoA:carnitine CoA-transferase
Systematic name:
(E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase

Reactions

Comments:

The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates. Formerly EC 4.2.1.89.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (34) [show] [UniProt]

References

  1. Engemann, C., Elssner, T., Kleber, H. P.
    Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
    Arch. Microbiol. 175 : 353-359 (2001). [PMID: 11409545]
  2. Elssner, T., Engemann, C., Baumgart, K., Kleber, H. P.
    Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli.
    Biochemistry 40 : 11140-11148 (2001). [PMID: 11551212]
  3. Stenmark, P., Gurmu, D., Nordlund, P.
    Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism.
    Biochemistry 43 : 13996-14003 (2004). [PMID: 15518548]
  4. Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T., Kleber, H. P.
    Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.
    Arch. Microbiol. 183 : 176-189 (2005). [PMID: 15731894]
  5. Rangarajan, E. S., Li, Y., Iannuzzi, P., Cygler, M., Matte, A.
    Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA.
    Biochemistry 44 : 5728-5738 (2005). [PMID: 15823031]

[EC 2.8.3.21 created 2014]