EzCatDB: D00091

DB codeD00091
CATH domainDomain 13.30.70.250
Domain 23.40.366.10Catalytic domain
E.C.2.3.1.39
CSA1mla
MACiEM0291


Enzyme Name
Swiss-protKEGG

P0AAI9
Protein nameMalonyl CoA-acyl carrier protein transacylase[acyl-carrier-protein] S-malonyltransferase
[acyl carrier protein]malonyltransferase
FabD
malonyl coenzyme A-acyl carrier protein transacylase
malonyl transacylase
malonyl transferase
malonyl-CoA-acyl carrier protein transacylase
malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase
malonyl-CoA:ACP transacylase
malonyl-CoA:ACP-SH transacylase
malonyl-CoA:AcpM transacylase
malonyl-CoA:acyl carrier protein transacylase
malonyl-CoA:acyl-carrier-protein transacylase
malonyl-CoA/dephospho-CoA acyltransferase
MAT
MCAT
MdcH
SynonymsMCT
EC 2.3.1.39

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis

Swiss-prot:Accession NumberP0AAI9
Entry nameFABD_ECOLI
ActivityMalonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
Subunit
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC00083C00229C00010C01209
CompoundMalonyl-CoAAcyl-carrier proteinCoAMalonyl-[acyl-carrier protein]
Typeamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide groupcarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl groupamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupcarbohydrate,carboxyl group,peptide/protein,phosphate group/phosphate ion,sulfide group
1mlaA01UnboundUnboundUnboundUnbound
1mlaA02UnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1mla & Swiss-prot;P0AAI9
pdbCatalytic residues
1mlaA01
1mlaA02SER  92;HIS 201

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.12962-12964

references
[1]
PubMed ID8078074
JournalJ Mol Biol
Year1994
Volume242
Pages99-102
AuthorsSerre L, Swenson L, Green R, Wei Y, Verwoert II, Verbree EC, Stuitje AR, Derewenda ZS
TitleCrystallization of the malonyl coenzyme A-acyl carrier protein transacylase from Escherichia coli.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID95286570
PubMed ID7768883
JournalJ Biol Chem
Year1995
Volume270
Pages12961-4
AuthorsSerre L, Verbree EC, Dauter Z, Stuitje AR, Derewenda ZS
TitleThe Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
Related PDB1mla
Related Swiss-protP0AAI9
[3]
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.
[4]
PubMed ID9862793
JournalChem Biol
Year1998
Volume5
Pages699-711
AuthorsMatharu AL, Cox RJ, Crosby J, Byrom KJ, Simpson TJ
TitleMCAT is not required for in vitro polyketide synthesis in a minimal actinorhodin polyketide synthase from Streptomyces coelicolor.
[5]
PubMed ID9632638
JournalJ Biol Chem
Year1998
Volume273
Pages15920-6
AuthorsWilson MC, Jackson VN, Heddle C, Price NT, Pilegaard H, Juel C, Bonen A, Montgomery I, Hutter OF, Halestrap AP
TitleLactic acid efflux from white skeletal muscle is catalyzed by the monocarboxylate transporter isoform MCT3.
[6]
PubMed ID10421763
JournalChem Biol
Year1999
Volume6
Pages577-84
AuthorsZhou P, Florova G, Reynolds KA
TitlePolyketide synthase acyl carrier protein (ACP) as a substrate and a catalyst for malonyl ACP biosynthesis.
[7]
PubMed ID10684659
JournalBiochemistry
Year2000
Volume39
Pages2088-95
AuthorsDreier J, Khosla C
TitleMechanistic analysis of a type II polyketide synthase. Role of conserved residues in the beta-ketoacyl synthase-chain length factor heterodimer.
[8]
PubMed ID11814333
JournalBiochemistry
Year2002
Volume41
Pages1421-7
AuthorsSzafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ
TitleKinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site.


createdupdated
2004-03-172012-06-01
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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