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Information on EC 2.8.3.19 - CoA:oxalate CoA-transferase and Organism(s) Escherichia coli and UniProt Accession P76518

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.19 CoA:oxalate CoA-transferase
IUBMB Comments
The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16, formyl-CoA transferase) or formyl-CoA and acetate, with significantly reduced specific activities.
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This record set is specific for:
Escherichia coli
UNIPROT: P76518
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
acoct, acetyl-coa:oxalate coa-transferase, acetyl-coenzyme a transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl-CoA:oxalate CoA transferase
-
acetyl-CoA:oxalate CoA-transferase
-
acetyl-CoA oxalate CoA-transferase
-
-
-
-
acetyl-coenzyme A transferase
-
-
-
-
ACOCT
-
-
-
-
UctC
-
-
-
-
YfdE
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:oxalate CoA-transferase
The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16, formyl-CoA transferase) or formyl-CoA and acetate, with significantly reduced specific activities.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + oxalyl-CoA
acetyl-CoA + oxalate
show the reaction diagram
-
-
-
?
oxalate + acetyl-CoA
oxalyl-CoA + acetate
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetate + oxalyl-CoA
acetyl-CoA + oxalate
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
acetyl-CoA
at pH 6.7 and 25°C
22
oxalate
at pH 6.7 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
acetyl-CoA
at pH 6.7 and 25°C
15
oxalate
at pH 6.7 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
650
acetyl-CoA
at pH 6.7 and 25°C
0.68
oxalate
at pH 6.7 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
at pH 6.7 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 20% (w/v) PEG 8000
hanging drop vapor diffusion method, using 0.1 M Tris-NHCl, pH 8.5, 0.2 M MgCl2, and 20% (w/v) PEG 8000
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Cibacron Blue 3GA column chromatography
ammonium sulfate precipitation, Ni-NTA column chromatography, and Cibacron Blue 3GA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) or C41(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mullins, E.A.; Sullivan, K.L.; Kappock, T.J.
Function and X-ray crystal structure of Escherichia coli YfdE
PLoS ONE
8
e67901
2013
Escherichia coli (P76518), Escherichia coli
Manually annotated by BRENDA team