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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.149 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.149 0.012
-
crotonobetainyl-CoA at pH 7.5 and 37°C Escherichia coli
4.2.1.149 0.038
-
crotonyl-CoA at pH 7.5 and 37°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.149 27000
-
x * 27000, SDS-PAGE Escherichia coli
4.2.1.149 87000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.149 crotonobetainyl-CoA + H2O Escherichia coli
-
L-carnitinyl-CoA
-
r
4.2.1.149 crotonyl-CoA + H2O Escherichia coli
-
?
-
?
4.2.1.149 L-carnitinyl-CoA Escherichia coli
-
crotonobetainyl-CoA + H2O
-
r
4.2.1.149 additional information Escherichia coli does not use crotonobetaine as substrate ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.21 Escherichia coli P31572
-
-
4.2.1.149 Escherichia coli P31551
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.149 DEAE-Sepharose column chromatography and Resource Q column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.8.3.21 187.8
-
pH 7.5, 37°C Escherichia coli
4.2.1.149 60.3
-
cell-free extract, at pH 7.5 and 37°C Escherichia coli
4.2.1.149 699.9
-
after 11.6fold purification, at pH 7.5 and 37°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.21 crotonobetainyl-CoA + L-carnitine
-
Escherichia coli crotonobetaine + L-carnitinyl-CoA
-
?
2.8.3.21 gamma-butyrobetainyl-CoA + L-carnitine
-
Escherichia coli gamma-butyrobetaine + L-carnitinyl-CoA
-
?
2.8.3.21 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 ?
-
?
4.2.1.149 crotonobetainyl-CoA + H2O
-
Escherichia coli L-carnitinyl-CoA
-
r
4.2.1.149 crotonyl-CoA + H2O
-
Escherichia coli ?
-
?
4.2.1.149 L-carnitinyl-CoA
-
Escherichia coli crotonobetainyl-CoA + H2O
-
r
4.2.1.149 additional information does not use crotonobetaine as substrate Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
4.2.1.149 ? x * 27000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.8.3.21 CaiB
-
Escherichia coli
4.2.1.149 CaiD
-
Escherichia coli