Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Engemann, C.; Elssner, T.; Kleber, H.P.
    Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp. (2001), Arch. Microbiol., 175, 353-359.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.3.21 43600
-
 2 * 43600, SDS-PAGE Proteus sp.
2.8.3.21 91100
-
 gel filtration Proteus sp.
4.2.1.149 43600
-
 2 * 43600, SDS-PAGE Proteus sp.
4.2.1.149 84200
-
 gel filtration Proteus sp.
4.2.1.149 91100
-
 calculated from amino acid sequence Proteus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.149 L-carnitinyl-CoA Proteus sp.
-
 (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.21 Proteus sp. Q8GB19
-
-
2.8.3.21 Proteus sp. LE138 Q8GB19
-
-
4.2.1.149 Proteus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.149 ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Resource Q column chromatography, and Superose 12HR gel filtration Proteus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.149 3
-
 cell free extract, in 10 mM sodium phosphate buffer (pH 7.8), at 37°C Proteus sp.
4.2.1.149 450
-
 after 150fold purification, in 10 mM sodium phosphate buffer (pH 7.8), at 37°C Proteus sp.

Storage Stability

EC Number Storage Stability Organism
4.2.1.149 0 or 20°C, purified enzyme in 50 mM sodium phosphate buffer containing 150 mM NaCl, 48 h, complete loss of activity Proteus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.21 (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
-
 Proteus sp. (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
-
 ?
2.8.3.21 (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
-
 Proteus sp. LE138 (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
-
 ?
2.8.3.21 4-trimethylammoniobutanoyl-CoA + L-carnitine
-
 Proteus sp. 4-trimethylammoniobutanoate + L-carnitinyl-CoA
-
 ?
2.8.3.21 4-trimethylammoniobutanoyl-CoA + L-carnitine
-
 Proteus sp. LE138 4-trimethylammoniobutanoate + L-carnitinyl-CoA
-
 ?
2.8.3.21 additional information enzyme CaiB alone is unable to convert crotonobetaine into L-(-)-carnitine even in the presence of the cosubstrates crotonobetainyl-CoA or gamma-butyrobetainyl-CoA, which are essential for this biotransformation. The presence of both CaiB and CaiD protein and cosubstrate crotonobetainyl-CoA or gamma-butyrobetainyl-CoA are essential Proteus sp. ?
-
 ?
2.8.3.21 additional information enzyme CaiB alone is unable to convert crotonobetaine into L-(-)-carnitine even in the presence of the cosubstrates crotonobetainyl-CoA or gamma-butyrobetainyl-CoA, which are essential for this biotransformation. The presence of both CaiB and CaiD protein and cosubstrate crotonobetainyl-CoA or gamma-butyrobetainyl-CoA are essential Proteus sp. LE138 ?
-
 ?
4.2.1.149 L-carnitinyl-CoA
-
 Proteus sp. (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.21 dimer 2 * 43600, SDS-PAGE Proteus sp.
4.2.1.149 homodimer 2 * 43600, SDS-PAGE Proteus sp.

Synonyms

EC Number Synonyms Comment Organism
2.8.3.21 CaiB
-
 Proteus sp.
2.8.3.21 crotonobetainyl-CoA:carnitine CoA-transferase
-
 Proteus sp.
4.2.1.149 CaiD
-
 Proteus sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.8.3.21 Proteus sp. isoelectric focusing
-
 5
4.2.1.149 Proteus sp. calculated from amino acid sequence
-
 5