EzCatDB: D00090

DB codeD00090
CATH domainDomain 13.40.47.10Catalytic domain
Domain 23.40.47.20Catalytic domain
E.C.2.3.1.16
CSA1afw
MACiEM0077

CATH domainRelated DB codes (homologues)
3.40.47.10D00411,D00509,D00825,D00826,D00867,D00871

Enzyme Name
Swiss-protKEGG

P27796
Protein name3-ketoacyl-CoA thiolase, peroxisomalacetyl-CoA C-acyltransferase
beta-ketothiolase
3-ketoacyl-CoA thiolase
KAT
beta-ketoacyl coenzyme A thiolase
beta-ketoacyl-CoA thiolase
beta-ketoadipyl coenzyme A thiolase
beta-ketoadipyl-CoA thiolase
3-ketoacyl CoA thiolase
3-ketoacyl coenzyme A thiolase
3-ketoacyl thiolase
3-ketothiolase
3-oxoacyl-CoA thiolase
3-oxoacyl-coenzyme A thiolase
6-oxoacyl-CoA thiolase
acetoacetyl-CoA beta-ketothiolase
acetyl-CoA acyltransferase
ketoacyl-CoA acyltransferase
ketoacyl-coenzyme A thiolase
long-chain 3-oxoacyl-CoA thiolase
oxoacyl-coenzyme A thiolase
pro-3-ketoacyl-CoA thiolase
thiolase I
2-methylacetoacetyl-CoA thiolase [misleading]
SynonymsEC 2.3.1.16
Beta-ketothiolase
Acetyl-CoA acyltransferase
Peroxisomal 3-oxoacyl-CoA thiolase

KEGG pathways
MAP codePathways
MAP00062Fatty acid elongation in mitochondria
MAP00071Fatty acid metabolism
MAP00120Bile acid biosynthesis
MAP00280Valine, leucine and isoleucine degradation
MAP00281Geraniol degradation
MAP00362Benzoate degradation via hydroxylation
MAP00592alpha-Linolenic acid metabolism
MAP00642Ethylbenzene degradation
MAP01040Biosynthesis of unsaturated fatty acids

Swiss-prot:Accession NumberP27796
Entry nameTHIK_YEAST
ActivityAcyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
SubunitHomodimer.
Subcellular locationPeroxisome.
Cofactor


SubstratesProducts
KEGG-idC00040C00024C00010C00264
CompoundAcyl-CoAAcetyl-CoACoA3-Oxoacyl-CoA
Typeamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupamine group,carbohydrate,nucleotide,peptide/protein,phosphate group/phosphate ion,sulfide group
1afwA01UnboundUnboundUnboundUnbound
1afwB01UnboundUnboundUnboundUnbound
1pxtA01UnboundUnboundUnboundUnbound
1pxtB01UnboundUnboundUnboundUnbound
1afwA02UnboundUnboundUnboundUnbound
1afwB02UnboundUnboundUnboundUnbound
1pxtA02UnboundUnboundUnboundUnbound
1pxtB02UnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1Swiss-prot;P27796
pdbCatalytic residues
1afwA01CYS 125
1afwB01CYS 125
1pxtA01CYS 125
1pxtB01CYS 125
1afwA02HIS 375;CYS 403
1afwB02HIS 375;CYS 403
1pxtA02HIS 375;CYS 403
1pxtB02HIS 375;CYS 403

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.800-801, p.804, Fig.13
[5]p.723, Fig.94

references
[1]
PubMed ID2859988
JournalEur J Biochem
Year1985
Volume149
Pages181-6
AuthorsMori M, Matsue H, Miura S, Tatibana M, Hashimoto T
TitleTransport of proteins into mitochondrial matrix. Evidence suggesting a common pathway for 3-ketoacyl-CoA thiolase and enzymes having presequences.
[2]
PubMed ID2213879
JournalJ Mol Biol
Year1990
Volume215
Pages211-3
AuthorsZeelen JP, Wierenga RK, Erdmann R, Kunau WH
TitleCrystallographic studies of 3-ketoacylCoA thiolase from yeast Saccharomyces cerevisiae.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID95111951
PubMed ID7812714
JournalStructure
Year1994
Volume2
Pages797-808
AuthorsMathieu M, Zeelen JP, Pauptit RA, Erdmann R, Kunau WH, Wierenga RK
TitleThe 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology.
Related PDB1pxt
Related Swiss-protP27796
[4]
PubMed ID7756275
JournalBiochemistry
Year1995
Volume34
Pages6441-7
AuthorsYang SY, He XY, Schulz H
TitleGlutamate 139 of the large alpha-subunit is the catalytic base in the dehydration of both D- and L-3-hydroxyacyl-coenzyme A but not in the isomerization of delta 3, delta 2-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID98022915
PubMed ID9402066
JournalJ Mol Biol
Year1997
Volume273
Pages714-28
AuthorsMathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK
TitleThe 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
Related PDB1afw,1afy
Related Swiss-protP27796
[6]
PubMed ID9215574
JournalProtein Eng
Year1997
Volume10
Pages561-6
AuthorsRangan VS, Serre L, Witkowska HE, Bari A, Smith S
TitleCharacterization of the malonyl-/acetyltransacylase domain of the multifunctional animal fatty acid synthase by expression in Escherichia coli and refolding in vitro.
[7]
PubMed ID9744475
JournalHum Mutat
Year1998
Volume12
Pages245-54
AuthorsFukao T, Nakamura H, Song XQ, Nakamura K, Orii KE, Kohno Y, Kano M, Yamaguchi S, Hashimoto T, Orii T, Kondo N
TitleCharacterization of N93S, I312T, and A333P missense mutations in two Japanese families with mitochondrial acetoacetyl-CoA thiolase deficiency.
[8]
PubMed ID10098837
JournalJ Neurochem
Year1999
Volume72
Pages1362-71
AuthorsBallestero RP, Dybowski JA, Levy G, Agranoff BW, Uhler MD
TitleCloning and characterization of zRICH, a 2',3'-cyclic-nucleotide 3'-phosphodiesterase induced during zebrafish optic nerve regeneration.
[9]
PubMed ID10727229
JournalBiochemistry
Year2000
Volume39
Pages3360-8
AuthorsVinarov DA, Miziorko HM
Title3-hydroxy-3-methylglutaryl-coenzyme A synthase reaction intermediates: detection of a covalent tetrahedral adduct by differential isotope shift 13C nuclear magnetic resonance spectroscopy.
[10]
PubMed ID11915938
JournalCell Mol Life Sci
Year2002
Volume59
Pages193-212
AuthorsStolowich NJ, Petrescu AD, Huang H, Martin GG, Scott AI, Schroeder F
TitleSterol carrier protein-2: structure reveals function.
[11]
PubMed ID11914035
JournalMol Genet Metab
Year2002
Volume75
Pages235-43
AuthorsFukao T, Nakamura H, Nakamura K, Perez-Cerda C, Baldellou A, Barrionuevo CR, Castello FG, Kohno Y, Ugarte M, Kondo N
TitleCharacterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure.


createdupdated
2004-03-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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