Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase and Organism(s) Candida tropicalis and UniProt Accession Q12598

for references in articles please use BRENDA:EC2.3.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Candida tropicalis
UNIPROT: Q12598
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Candida tropicalis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
acetoacetyl-coa thiolase, acetyl-coa acetyltransferase, erg10, acoat, acetyl-coa c-acetyltransferase, cytosolic acetoacetyl-coa thiolase, 2-methylacetoacetyl-coa thiolase, osat1, acetoacetyl coa thiolase, aact2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-methylacetoacetyl-CoA thiolase
-
-
-
-
3-oxothiolase
-
-
-
-
acetoacetyl CoA thiolase
-
-
-
-
acetoacetyl-CoA thiolase
-
-
-
-
acetyl coenzyme A thiolase
-
-
-
-
acetyl-CoA acetyltransferase
-
-
-
-
acetyl-CoA:N-acetyltransferase
-
-
-
-
acetyltransferase, acetyl coenzyme A
-
-
-
-
beta-acetoacetyl coenzyme A thiolase
-
-
-
-
thiolase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
Acyl group transfer
-
-
-
-
thiolytic cleavage
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-46-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
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
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.057
acetoacetyl-CoA
0.69 - 1.05
acetyl-CoA
0.03 - 0.05
CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
-
cytosolic and peroxisomal thiolase I, synthesis
8.3
-
cytosolic and peroxisomal thiolase I
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
N-terminal sequence targets thiolase I to the peroxisome
Manually annotated by BRENDA team
-
cytosolic thiolase I
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THIA_CANTR
403
0
41898
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
240000
-
peroxisomal thiolase I, gel filtration
250000
-
cytosolic thiolase I, gel filtration
41000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic thiolase I
-
DEAE-Sepharose, butyl-Toyopearl, Cellulofine
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of cytosolic and peroxisomal thiolase I in Saccharomyces cerevisiae
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurihara, T.; Ueda, M.; Tanaka, A.
Peroxisomal acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase from an n-alkane-utilizing yeast, Candida tropicalis: purification and characterization
J. Biochem.
106
474-478
1989
Candida tropicalis
Manually annotated by BRENDA team
Kanayama, N.; Ueda, M.; Atomi, H.; Tanaka, A.
Genetic evaluation of physiological functions of thiolase isoenzymes in the n-alkane-assimilating yeast Candida tropicalis
J. Bacteriol.
180
690-698
1998
Candida tropicalis (Q12598), Candida tropicalis
Manually annotated by BRENDA team
Kanayama, N.; Himeda, Y.; Atomi, H.; Ueda, M.; Tanaka, A.
Expression of acetoacetyl-CoA thiolase isoenzyme genes of n-alkane-assimilating yeast, Candida tropicalis: isoenzymes in two intracellular compartments are derived from the same genes
J. Biochem.
122
616-621
1997
Candida tropicalis, Rhizobium sp.
Manually annotated by BRENDA team