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Information on EC 2.8.3.21 - L-carnitine CoA-transferase and Organism(s) Proteus sp. and UniProt Accession Q8GB19

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.21 L-carnitine CoA-transferase
IUBMB Comments
The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates.
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This record set is specific for:
Proteus sp.
UNIPROT: Q8GB19
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The taxonomic range for the selected organisms is: Proteus sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
crotonobetainyl/gamma-butyrobetainyl-coa:carnitine coa-transferase, crotonobetainyl-coa:carnitine coa-transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
crotonobetainyl-CoA:carnitine CoA-transferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
show the reaction diagram
sequential bisubstrate mechanism
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase
The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
(E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
show the reaction diagram
-
-
-
?
4-trimethylammoniobutanoyl-CoA + L-carnitine
4-trimethylammoniobutanoate + L-carnitinyl-CoA
show the reaction diagram
-
-
-
?
crotonobetainyl-CoA + L-carnitine
crotonobetaine + L-carnitinyl-CoA
show the reaction diagram
-
-
-
?
gamma-butyrobetainyl-CoA + L-carnitine
gamma-butyrobetaine + L-carnitinyl-CoA
show the reaction diagram
-
-
-
?
additional information
?
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
556.3
pH 7.8, 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43600
2 * 43600, SDS-PAGE
91100
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 43600, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Proteus sp. (Q8GB19), Proteus sp. LE138 (Q8GB19)
Manually annotated by BRENDA team
Engemann, C.; Elssner, T.; Kleber, H.P.
Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
Arch. Microbiol.
175
353-359
2001
Proteus sp. (Q8GB19), Proteus sp. LE138 (Q8GB19)
Manually annotated by BRENDA team