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Information on EC 2.8.3.21 - L-carnitine CoA-transferase and Organism(s) Escherichia coli and UniProt Accession P31572

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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:
Escherichia coli
UNIPROT: P31572
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The taxonomic range for the selected organisms is: Escherichia coli
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/gamma-butyrobetainyl-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
(1)
4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
show the reaction diagram
(2)
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
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
187.8
pH 7.5, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
sitting-drop vapor-diffusion method, hanging-drop vapor-diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D169A
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stenmark, P.; Gurmu, D.; Nordlund, P.
Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism
Biochemistry
43
13996-14003
2004
Escherichia coli (P31572)
Manually annotated by BRENDA team
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
Biochemistry
40
11140-11148
2001
Escherichia coli (P31572), Escherichia coli
Manually annotated by BRENDA team
Rangarajan, E.S.; Li, Y.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA
Biochemistry
44
5728-5738
2005
Escherichia coli (P31572), Escherichia coli
Manually annotated by BRENDA team
Sevilla, A.; Vera, J.; Diaz, Z.; Canovas, M.; Torres, N.V.; Iborra, J.L.
Design of metabolic engineering strategies for maximizing L-(-)-carnitine production by Escherichia coli. Integration of the metabolic and bioreactor levels
Biotechnol. Prog.
21
329-337
2005
Escherichia coli
Manually annotated by BRENDA team
Bernal, V.; Masdemont, B.; Arense, P.; Canovas, M.; Iborra, J.L.
Redirecting metabolic fluxes through cofactor engineering: Role of CoA-esters pool during L(-)-carnitine production by Escherichia coli
J. Biotechnol.
132
110-117
2007
Escherichia coli
Manually annotated by BRENDA team