Information on EC 2.8.3.21 - L-carnitine CoA-transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.3.21
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RECOMMENDED NAME
GeneOntology No.
L-carnitine CoA-transferase
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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
4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-carnitine degradation I
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carnitine metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
187.8
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pH 7.5, 37°C
556.3
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pH 7.8, 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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isoelectric focusing
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43600
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2 * 43600, SDS-PAGE
91100
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB
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sitting-drop vapor-diffusion method, hanging-drop vapor-diffusion method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D169A
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utation of the predicted key catalytic residue. Upon cocrystallization with crotonoyl-CoA, electron density is observed only for the CoA region of the cofactor, ending at the sulfur atom as for the wild-type enzyme. When both carnitine and crotonoyl-CoA are cocrystallized with the mutant enzyme, the electron density observed in the binding site is consistent with formation of the product, carnitinyl-CoA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (362 entries)
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