EzCatDB: M00188

DB codeM00188
RLCP classification3.1177.805.87
CATH domainDomain 12.40.50.100
Domain 2-.-.-.-
Domain 34.10.320.10
Domain 43.30.559.10Catalytic domain
E.C.2.3.1.12
MACiEM0106

CATH domainRelated DB codes (homologues)
2.40.50.100M00163,M00222,M00145,M00189,T00223,M00190,M00191,M00208
3.30.559.10M00189,T00223,M00190,M00191
4.10.320.10M00189,T00223,M00190,M00191

Enzyme Name
Swiss-protKEGG

P11961
Protein nameDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexdihydrolipoyllysine-residue acetyltransferase
acetyl-CoA:dihydrolipoamide S-acetyltransferase
dihydrolipoamide S-acetyltransferase
dihydrolipoate acetyltransferase
dihydrolipoic transacetylase
dihydrolipoyl acetyltransferase
lipoate acetyltransferase
lipoate transacetylase
lipoic acetyltransferase
lipoic acid acetyltransferase
lipoic transacetylase
lipoylacetyltransferase
thioltransacetylase A
transacetylase X
enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase
acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase
SynonymsEC 2.3.1.12
E2
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00020Citrate cycle (TCA cycle)
MAP00620Pyruvate metabolism

Swiss-prot:Accession NumberP11961
Entry nameODP2_BACST
ActivityAcetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
SubunitForms a 60-polypeptide structural core with icosahedral symmetry.
Subcellular location
CofactorBinds 1 lipoyl cofactor covalently.


SubstratesProducts
KEGG-idC00010L00017C00024C15973
CompoundCoAEnzyme N(6)-(S-acetyldihydrolipoyl)lysineAcetyl-CoAEnzyme N(6)-(dihydrolipoyl)lysine
Typeamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupamide group,carbohydrate,lipid,peptide/protein,sulfhydryl group,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamide group,lipid,peptide/protein,sulfhydryl group
1labAUnboundUnboundUnboundUnbound
1lacAUnboundUnboundUnboundUnbound
1ebdCUnboundUnboundUnboundUnbound
1w3dAUnboundUnboundUnboundUnbound
1w4eAUnboundUnboundUnboundUnbound
1w4fAUnboundUnboundUnboundUnbound
1w4gAUnboundUnboundUnboundUnbound
1w85IUnboundUnboundUnboundUnbound
1w85JUnboundUnboundUnboundUnbound
1w88IUnboundUnboundUnboundUnbound
1w88JUnboundUnboundUnboundUnbound
2pddAUnboundUnboundUnboundUnbound
1b5sAUnboundUnboundUnboundUnbound
1b5sBUnboundUnboundUnboundUnbound
1b5sCUnboundUnboundUnboundUnbound
1b5sDUnboundUnboundUnboundUnbound
1b5sEUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1fyc, 1iyu, 1lab
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
1labA
LYS  42(Lipoyl binding)

1lacA
LYS  42(Lipoyl binding)

1ebdC


1w3dA


1w4eA


1w4fA


1w4gA


1w85I


1w85J


1w88I


1w88J


2pddA


1b5sAARG 206;THR 346;HIS 398;ASP 402

HIS 398
1b5sBARG 206;THR 346;HIS 398;ASP 402

HIS 398
1b5sCARG 206;THR 346;HIS 398;ASP 402

HIS 398
1b5sDARG 206;THR 346;HIS 398;ASP 402

HIS 398
1b5sEARG 206;THR 346;HIS 398;ASP 402

HIS 398


references
[1]
PubMed ID6345153
JournalEur J Biochem
Year1983
Volume133
Pages481-9
AuthorsStephens PE, Darlison MG, Lewis HM, Guest JR
TitleThe pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component
[2]
PubMed ID6090132
JournalEur J Biochem
Year1984
Volume143
Pages561-6
AuthorsSchrenk DF, Bisswanger H
TitleMeasurements of electron spin resonance with the pyruvate dehydrogenase complex from Escherichia coli. Studies on the allosteric binding site of acetyl-coenzyme A
[3]
PubMed ID3903169
JournalJ Mol Biol
Year1985
Volume185
Pages743-54
AuthorsGuest JR, Lewis HM, Graham LD, Packman LC, Perham RN
TitleGenetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
[4]
PubMed ID3691494
JournalEur J Biochem
Year1987
Volume169
Pages245-52
AuthorsHanemaaijer R, de Kok A, Jolles J, Veeger C
TitleThe domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
[5]
PubMed ID2917567
JournalEur J Biochem
Year1989
Volume179
Pages287-92
AuthorsHanemaaijer R, Westphal AH, Van Der Heiden T, De Kok A, Veeger C
TitleThe quaternary structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. A reconsideration.
[6]
PubMed ID2684741
JournalFEMS Microbiol Lett
Year1989
Volume51
Pages267-71
AuthorsRussell GC, Williamson RA, Guest JR
TitlePartial complementation of pyruvate dehydrogenase deficiency by independently expressed lipoyl and catalytic domains of the dihydrolipoamide acetyltransferase component
[7]
PubMed ID2271545
JournalBiochemistry
Year1990
Volume29
Pages8614-9
AuthorsNiu XD, Stoops JK, Reed LJ
TitleOverexpression and mutagenesis of the catalytic domain of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae
[8]
CommentsSTRUCTURE BY NMR OF 1-85.
Medline ID92007876
PubMed ID1915365
JournalEur J Biochem
Year1991
Volume201
Pages203-9
AuthorsDardel F, Laue ED, Perham RN
TitleSequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
Related Swiss-protP11961
[9]
PubMed ID1676519
JournalProc R Soc Lond B Biol Sci
Year1991
Volume243
Pages155-60
AuthorsRussell GC, Guest JR
TitleSite-directed mutagenesis of the lipoate acetyltransferase of Escherichia coli.
[10]
PubMed ID1590756
JournalBiochem J
Year1992
Volume283
Pages665-71
AuthorsHipps DS, Perham RN
TitleExpression in Escherichia coli of a sub-gene encoding the lipoyl and peripheral subunit-binding domains of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus
[11]
CommentsSTRUCTURE BY NMR OF 1-85.
Medline ID93187999
PubMed ID8445635
JournalJ Mol Biol
Year1993
Volume229
Pages1037-48
AuthorsDardel F, Davis AL, Laue ED, Perham RN
TitleThree-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
Related PDB1lab,1lac
Related Swiss-protP11961
[12]
CommentsSTRUCTURE BY NMR OF 128-170.
Medline ID93195938
PubMed ID8450544
JournalJ Mol Biol
Year1993
Volume230
Pages323-41
AuthorsKalia YN, Brocklehurst SM, Hipps DS, Appella E, Sakaguchi K, Perham RN
TitleThe high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
Related PDB2pdd
Related Swiss-protP11961
[13]
PubMed ID8433963
JournalProtein Eng
Year1993
Volume6
Pages101-8
AuthorsTurner SL, Russell GC, Williamson MP, Guest JR
TitleRestructuring an interdomain linker in the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli
[14]
PubMed ID8206840
JournalJ Bacteriol
Year1994
Volume176
Pages3614-30
AuthorsKruger N, Oppermann FB, Lorenzl H, Steinbuchel A
TitleBiochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system.
[15]
PubMed ID8107106
JournalJ Mol Biol
Year1994
Volume236
Pages209-16
AuthorsWallis NG, Perham RN
TitleStructural dependence of post-translational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 128-170.
Medline ID96398614
PubMed ID8805537
JournalStructure
Year1996
Volume4
Pages277-86
AuthorsMande SS, Sarfaty S, Allen MD, Perham RN, Hol WG
TitleProtein-protein interactions in the pyruvate dehydrogenase multienzyme complex
Related PDB1ebd
Related Swiss-protP11961
[17]
PubMed ID9043123
JournalMicrobiology
Year1997
Volume143
Pages457-66
AuthorsGuest JR, Attwood MM, Machado RS, Matqi KY, Shaw JE, Turner SL
TitleEnzymological and physiological consequences of restructuring the lipoyl domain content of the pyruvate dehydrogenase complex of Escherichia coli.
[18]
CommentsX-ray crystallography
PubMed ID9990008
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages1240-5
AuthorsIzard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG
TitlePrinciples of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes.
Related PDB1b5s
[19]
PubMed ID15514159
JournalScience
Year2004
Volume306
Pages872-6
AuthorsFrank RA, Titman CM, Pratap JV, Luisi BF, Perham RN
TitleA molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Related PDB1w85,1w88
[20]
PubMed ID15634348
JournalFEBS J
Year2005
Volume272
Pages259-68
AuthorsAllen MD, Broadhurst RW, Solomon RG, Perham RN
TitleInteraction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy.
Related PDB1w3d
[21]
PubMed ID16168437
JournalJ Mol Biol
Year2005
Volume353
Pages427-46
AuthorsFerguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR
TitleUltra-fast barrier-limited folding in the peripheral subunit-binding domain family.
Related PDB1w4e,1w4f,1w4g,1w4h,2btg,2bth
[22]
PubMed ID16406408
JournalJ Mol Biol
Year2006
Volume356
Pages1237-47
AuthorsFerguson N, Sharpe TD, Johnson CM, Fersht AR
TitleThe transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics.
Related PDB1w4e,1w4f,1w4g

comments
This enzyme is Dihydrolipoyllysine-residue acetyltransferase, E2 component of pyruvate dehydrogenase complex.
The pyruvate dehydrogenase complex is composed of pyruvate dehydrogenaes (E1 component; E.C. 1.2.4.1), dihydrolipoyllysine S-acetyltransferase (E2 component; E.C. 2.3.1.12), and lipoamide dehydrogenase (E3 component; E.C. 1.8.1.4). (The E3 component corresponds to the entry T00017 in EzCatDB.)
This enzyme is composed of the N-terminal lipoyl-binding domain, E3-binding domain, and the C-terminal catalytic domain.
This enzyme catalyzes transfer of acetyl group from lypoyllysine of the lipoyl-binding domain to thiol group of CoA.
The catalytic domain of this enzyme is homologous to that of dihydrolipoamide succinyltransferase (E.C. 2.3.1.61; T00223 in EzCatDB). The catalytic residues seem to be conserved between these two enzymes. Thus, the catalytic mechanism must be the same as that of the homologue.

createdupdated
2004-03-192009-09-29


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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