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Literature summary for 2.8.3.21 extracted from

  • 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 (2001), Biochemistry, 40, 11140-11148.
    View publication on PubMed
Search for more literature for 2.8.3.21

Organism

Organism UniProt Comment Textmining
Escherichia coli P31572
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-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
187.8
-
 pH 7.5, 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonobetainyl-CoA + L-carnitine
-
 Escherichia coli crotonobetaine + L-carnitinyl-CoA
-
 ?
gamma-butyrobetainyl-CoA + L-carnitine
-
 Escherichia coli gamma-butyrobetaine + L-carnitinyl-CoA
-
 ?
additional information enzyme exhibits high cosubstrate specificity to CoA derivatives of trimethylammonium compounds. Hydration of crotonobetaine to L-carnitine proceeds at the CoA level in two steps: the CaiD catalyzed hydration of crotonobetainyl-CoA to L-carnitinyl-CoA, followed by a CoA transfer from L-carnitinyl-CoA to crotonobetaine, catalyzed by transferase CaiB. When gamma-butyrobetainyl-CoA is used as a cosubstrate, the first reaction is the CoA transfer. The optimal ratios of CaiB and CaiD during this hydration reaction, determined to be 4:1 when crotonobetainyl-CoA is used as cosubstrate and 5:1 when gamma-butyrobetainyl-CoA is used as cosubstrate, are different from that found for in vivo conditions, i.e. 1:3 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
CaiB
-
 Escherichia coli