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Information on EC 2.8.3.8 - acetate CoA-transferase and Organism(s) Escherichia coli and UniProt Accession P76458

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.8 acetate CoA-transferase
IUBMB Comments
The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate---acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA.
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This record set is specific for:
Escherichia coli
UNIPROT: P76458
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
butyryl-coa:acetate coa-transferase, butyryl-coa acetate coa-transferase, acetate:succinate coa-transferase, butyryl-coenzyme a coa transferase, acetate coa-transferase, acyl-coa:acetate coa-transferase, acetoacetate:acetate coa-transferase, succinyl-coa:acetate coa transferase, butyryl coa:acetate coa transferase, butyryl coenzyme a transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetate coenzyme A-transferase
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butyryl CoA:acetate CoA transferase
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butyryl coenzyme A transferase
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coenzyme A-transferase, acetate
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succinyl-CoA:acetate CoA transferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetate CoA-transferase
The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate---acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-35-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
butanoyl-CoA + acetate
?
show the reaction diagram
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provides ability to grow on various fatty acids
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-
r
butanoyl-CoA + acetate
butanoate + acetyl-CoA
show the reaction diagram
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best substrate
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r
pentanoyl-CoA + acetate
pentanoate + acetyl-CoA
show the reaction diagram
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-
-
-
r
valeryl-CoA + acetate
valerate + acetyl-CoA
show the reaction diagram
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-
-
-
r
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
butanoyl-CoA + acetate
?
show the reaction diagram
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provides ability to grow on various fatty acids
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-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains 3 Mg2+ ions, none of them located near the putative active site, functional relevance is not clear
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1 - 1
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in crude cell extract
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
alpha subunit assembles as a dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, alpha subunit, native enzyme and SeMet-derivatized protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
98% pure, alpha subunit
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vanderwinkel, E.; Furmanski, P.; Reeves, H.C.; Ajl, S.J.
Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity
Biochem. Biophys. Res. Commun.
33
902-908
1968
Escherichia coli
Manually annotated by BRENDA team
Korolev, S.; Koroleva, O.; Petterson, K.; Gu, M.; Collart, F.; Dementieva, I.; Joachimiak, A.
Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data
Acta Crystallogr. Sect. D
58
2116-2121
2002
Escherichia coli (P76458), Escherichia coli
Manually annotated by BRENDA team