DB code: D00256

CATH domain 1.10.580.10 : Citrate Synthase; domain 1 Catalytic domain
1.10.230.10 : Cytochrome p450-Terp; domain 2 Catalytic domain
E.C. 2.3.3.1
CSA 1al6 1aj8
M-CSA 1al6 1aj8
MACiE M0078

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q53554 Citrate synthase
EC 2.3.3.1
NP_577932.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
PF00285 (Citrate_synt)
[Graphical View]
P23007 Citrate synthase, mitochondrial
EC 2.3.3.1
PF00285 (Citrate_synt)
[Graphical View]
P00889 Citrate synthase, mitochondrial
EC 2.3.3.1
NP_999441.1 (Protein)
NM_214276.1 (DNA/RNA sequence)
PF00285 (Citrate_synt)
[Graphical View]

KEGG enzyme name
citrate (Si)-synthase
(R)-citric synthase
citrate condensing enzyme
citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]
citrate oxaloacetate-lyase, CoA-acetylating
citrate synthase
citrate synthetase
citric synthase
citric-condensing enzyme
citrogenase
condensing enzyme
oxaloacetate transacetase
oxalacetic transacetase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q53554 CISY_PYRFU Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. Homodimer.
P23007 CISY_CHICK Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. Homodimer. Mitochondrion matrix.
P00889 CISY_PIG Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. Homodimer. Mitochondrion matrix.

KEGG Pathways
Map code Pathways E.C.
MAP00020 Citrate cycle (TCA cycle)
MAP00630 Glyoxylate and dicarboxylate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00024 C00001 C00036 C00010 C00158 C00566
E.C.
Compound Acetyl-CoA H2O Oxaloacetate CoA Citrate Enolic acetyl-CoA Citryl-CoA Enzyme-anhydride intermediate
Type amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group H2O carbohydrate,carboxyl group amine group,carbohydrate,nucleotide ,peptide/protein,sulfhydryl group carbohydrate,carboxyl group
ChEBI 15351
15377
30744
15346
30769
PubChem 444493
6302
22247451
962
970
6816
87642
19782904
311
88113319
1aj8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1aj8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1al6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1amzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cshA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1csiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1csrA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cssA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
4cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
5cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
5cscB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
5ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
6cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
6cscB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
6ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
4ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
4ctsB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1aj8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:COA Bound:CIT Unbound
1aj8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:COA Bound:CIT Unbound
1al6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HAX Bound:OAA Unbound Unbound Unbound
1amzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:NMX Analogue:MLT Unbound Unbound Unbound
1cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:CMC Analogue:MAL Unbound Unbound Unbound
1cshA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:AMX Bound:OAA Unbound Unbound Unbound
1csiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:CMX Bound:OAA Unbound Unbound Unbound
1csrA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:FAM Bound:OAA Unbound Unbound Unbound
1cssA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:FCX Bound:OAA Unbound Unbound Unbound
2cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:CMC Analogue:MAL Unbound Unbound Unbound
3cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:ACO Analogue:MAL Unbound Unbound Unbound
4cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:ACO Analogue:MAL Unbound Unbound Unbound
5cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
5cscB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
5ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:CMC Bound:OAA Unbound Unbound Unbound
6cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:COF Unbound Unbound Bound:CIT Unbound
6cscB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:COF Unbound Unbound Bound:CIT Unbound
6ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:CIC
1ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:COA Bound:CIT Unbound
4ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:OAA Unbound Unbound Unbound
4ctsB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:OAA Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P23007, P00889, Q53554

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1aj8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 223
1aj8B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 223
1al6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1amzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1cshA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1csiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1csrA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1cssA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
2cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
3cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
4cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
5cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
5cscB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
5ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
6cscA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
6cscB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
6ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
2ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
4ctsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
4ctsB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 274
1aj8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 262;ASP 312
1aj8B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 262;ASP 312
1al6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1amzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1cshA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1csiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1csrA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1cssA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
2cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
3cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
4cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
5cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
5cscB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
5ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
6cscA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
6cscB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
6ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375
1ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375 LYS 368(N6,N6,N6-trimethyllysine)
2ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375 LYS 368(N6,N6,N6-trimethyllysine)
4ctsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375 LYS 368(N6,N6,N6-trimethyllysine)
4ctsB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 320;ASP 375 LYS 368(N6,N6,N6-trimethyllysine)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
p.149-150
[7]
Scheme 2, p.671 2
[14]
Fig.3, p.7561-7562 4
[15]
Fig.4, p.2216 2
[16]
Scheme 3, p.711-712 3
[17]
Scheme 2, p.524-526 3
[18]
p.6030
[21]
p.7912-7914
[22]
p.7906-7907
[23]
Scheme 2, Scheme 3, Scheme 4, p.226 5
[27]
p.769-770
[29]
Fig.2, p.7757-7759 3
[35]
Fig.1, p.10667-10671 3
[39]
p.9987
[45]

References
[1]
Resource
Comments
Medline ID
PubMed ID 1278369
Journal FEBS Lett
Year 1976
Volume 62
Pages 281-3
Authors Wiegand G
Title Crystallization and preliminary x-ray data of well-ordered crystals from pig heart citrate synthase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 666830
Journal Biochem Biophys Res Commun
Year 1978
Volume 82
Pages 150-6
Authors Wang AH, Sherman ML, Rich A
Title A crystallographic investigation of citrate synthase from pig and chicken heart muscle.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 224920
Journal Biochemistry
Year 1979
Volume 18
Pages 3822-7
Authors Weidman SW, Drysdale GR
Title Interaction of a paramagnetic analogue of oxaloacetate with citrate synthase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 436830
Journal Eur J Biochem
Year 1979
Volume 93
Pages 41-50
Authors Wiegand G, Kukla D, Scholze H, Jones TA, Huber R
Title Crystal structure analysis of the tetragonal crystal form are preliminary molecular model of pig-heart citrate synthase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 218954
Journal J Biol Chem
Year 1979
Volume 254
Pages 2800-6
Authors Caggiano AV, Powell GL
Title Regulation of enzymes by fatty acyl coenzyme A. Site-specific binding of fatty acyl coenzyme A by citrate synthase--a spin-labeling study.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 AND 1.7 ANGSTROMS).
Medline ID 83010291
PubMed ID 7120407
Journal J Mol Biol
Year 1982
Volume 158
Pages 111-52
Authors Remington S, Wiegand G, Huber R
Title Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution.
Related PDB 1cts 2cts
Related UniProtKB P00889
[7]
Resource
Comments
Medline ID
PubMed ID 6861748
Journal Eur J Biochem
Year 1983
Volume 133
Pages 665-72
Authors Lohlein-Werhahn G, Bayer E, Bauer B, Eggerer H
Title Hysteretic behaviour of citrate synthase. Alternating sites during the catalytic cycle.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 6337135
Journal J Biol Chem
Year 1983
Volume 258
Pages 1297-8
Authors Rubin BH, Stallings WC, Glusker JP, Bayer ME, Janin J, Srere PA
Title Crystallographic studies of Escherichia coli citrate synthase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 6716477
Journal J Mol Biol
Year 1984
Volume 174
Pages 205-19
Authors Wiegand G, Remington S, Deisenhofer J, Huber R
Title Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A.
Related PDB 4cts
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 3978085
Journal Biochemistry
Year 1985
Volume 24
Pages 452-7
Authors Kurz LC, Ackerman JJ, Drysdale GR
Title Evidence from 13C NMR for polarization of the carbonyl of oxaloacetate in the active site of citrate synthase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 3607038
Journal Biochemistry
Year 1987
Volume 26
Pages 2623-7
Authors Kurz LC, Drysdale GR
Title Evidence from Fourier transform infrared spectroscopy for polarization of the carbonyl of oxaloacetate in the active site of citrate synthase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 2731546
Journal Eur J Biochem
Year 1989
Volume 182
Pages 119-24
Authors Pettersson G, Lill U, Eggerer H
Title Mechanism of interaction of citrate synthase with citryl-CoA.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 2276456
Journal Biochem Soc Trans
Year 1990
Volume 18
Pages 596-7
Authors Iles RA, Davies SE, Chalmers RA, Wharton CW, White A, Sreedharan S, Phillips I, Brocklehurst K
Title Structural and mechanistic studies on citrate synthase by nuclear magnetic resonance and Fourier transform infra-red spectroscopies.
Related PDB
Related UniProtKB
[14]
Resource
Comments MUTAGENESIS.
Medline ID 91104711
PubMed ID 1702991
Journal Biochemistry
Year 1990
Volume 29
Pages 7557-63
Authors Alter GM, Casazza JP, Zhi W, Nemeth P, Srere PA, Evans CT
Title Mutation of essential catalytic residues in pig citrate synthase.
Related PDB
Related UniProtKB P00889
[15]
Resource
Comments TISSUE=Heart muscle;
Medline ID 90248434
PubMed ID 2337600
Journal Biochemistry
Year 1990
Volume 29
Pages 2213-9
Authors Karpusas M, Branchaud B, Remington SJ
Title Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A.
Related PDB 5cts 6cts
Related UniProtKB P23007
[16]
Resource
Comments
Medline ID
PubMed ID 2206458
Journal Biol Chem Hoppe Seyler
Year 1990
Volume 371
Pages 707-13
Authors Wilde J, Lill U, Eggerer H
Title On the action of carboxy groups in the citrate synthase reaction.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 1684105
Journal Biochem J
Year 1991
Volume 280
Pages 521-6
Authors Man WJ, Li Y, O'Connor CD, Wilton DC
Title Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid.
Related PDB
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2043640
Journal Biochemistry
Year 1991
Volume 30
Pages 6024-31
Authors Karpusas M, Holland D, Remington SJ
Title 1.9-A structures of ternary complexes of citrate synthase with D- and L-malate: mechanistic implications.
Related PDB 1csc 2csc 3csc 4csc
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OPEN CONFORMATION.
Medline ID 91255228
PubMed ID 2043641
Journal Biochemistry
Year 1991
Volume 30
Pages 6031-6
Authors Liao DI, Karpusas M, Remington SJ
Title Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution.
Related PDB 5csc
Related UniProtKB P23007
[20]
Resource
Comments
Medline ID
PubMed ID 1939121
Journal J Biol Chem
Year 1991
Volume 266
Pages 20709-13
Authors Donald LJ, Crane BR, Anderson DH, Duckworth HW
Title The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 1324723
Journal Biochemistry
Year 1992
Volume 31
Pages 7908-14
Authors Kurz LC, Drysdale GR, Riley MC, Evans CT, Srere PA
Title Catalytic strategy of citrate synthase: effects of amino acid changes in the acetyl-CoA binding site on transition-state analog inhibitor complexes.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 1324722
Journal Biochemistry
Year 1992
Volume 31
Pages 7899-907
Authors Kurz LC, Shah S, Crane BR, Donald LJ, Duckworth HW, Drysdale GR
Title Proton uptake accompanies formation of the ternary complex of citrate synthase, oxaloacetate, and the transition-state analog inhibitor, carboxymethyl-CoA. Evidence that a neutral enol is the activated form of acetyl-CoA in the citrate synthase reaction.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 1499334
Journal Curr Top Cell Regul
Year 1992
Volume 33
Pages 209-29
Authors Remington SJ
Title Structure and mechanism of citrate synthase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 8098211
Journal Biochem J
Year 1993
Volume 291
Pages 927-32
Authors Evans CT, Sumegi B, Srere PA, Sherry AD, Malloy CR
Title 13C]propionate oxidation in wild-type and citrate synthase mutant Escherichia coli: evidence for multiple pathways of propionate utilization.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8331668
Journal J Mol Biol
Year 1993
Volume 232
Pages 308-9
Authors Russell RJ, Byrom D, Danson MJ, Hough DW, Taylor GL
Title Crystallization and preliminary crystallographic study of citrate synthase from the thermophilic Archaeon Thermoplasma acidophilum.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 8356034
Journal Proteins
Year 1993
Volume 16
Pages 393-407
Authors Ech-Cherif el-Kettani MA, Zakrzewska K, Durup J, Lavery R
Title An analysis of the conformational paths of citrate synthase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 8010958
Journal Biochem J
Year 1994
Volume 300
Pages 765-70
Authors Man WJ, Li Y, O'Connor CD, Wilton DC
Title The effect of replacing the conserved active-site residues His-264, Asp-312 and Arg-314 on the binding and catalytic properties of Escherichia coli citrate synthase.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 7918384
Journal Biochemistry
Year 1994
Volume 33
Pages 11684-91
Authors Lindbladh C, Brodeur RD, Small WC, Lilius G, Bulow L, Mosbach K, Srere PA
Title Metabolic studies on Saccharomyces cerevisiae containing fused citrate synthase/malate dehydrogenase.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8011640
Journal Biochemistry
Year 1994
Volume 33
Pages 7753-9
Authors Usher KC, Remington SJ, Martin DP, Drueckhammer DG
Title A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase.
Related PDB 1csh 1csi
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 8276829
Journal J Biol Chem
Year 1994
Volume 269
Pages 412-7
Authors Pereira DS, Donald LJ, Hosfield DJ, Duckworth HW
Title Active site mutants of Escherichia coli citrate synthase. Effects of mutations on catalytic and allosteric properties.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 7704526
Journal Structure
Year 1994
Volume 2
Pages 1157-67
Authors Russell RJ, Hough DW, Danson MJ, Taylor GL
Title The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 7577912
Journal Biochemistry
Year 1995
Volume 34
Pages 13278-88
Authors Kurz LC, Shah S, Frieden C, Nakra T, Stein RE, Drysdale GR, Evans CT, Srere PA
Title Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site.
Related PDB
Related UniProtKB
[33]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7492547
Journal Biochemistry
Year 1995
Volume 34
Pages 15459-66
Authors Schwartz B, Drueckhammer DG, Usher KC, Remington SJ
Title alpha-Fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of citrate synthase: effect of pKa matching on binding affinity and hydrogen bond length.
Related PDB 1csr 1css
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 9052973
Journal J Mol Recognit
Year 1995
Volume 8
Pages 327-33
Authors Evans CT
Title Metabolic engineering of a non-allosteric citrate synthase in an Escherichia coli citrate synthase mutant.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 8718855
Journal Biochemistry
Year 1996
Volume 35
Pages 10661-72
Authors Evans CT, Kurz LC, Remington SJ, Srere PA
Title Active site mutants of pig citrate synthase: effects of mutations on the enzyme catalytic and structural properties.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 8979399
Journal Plant Cell Physiol
Year 1996
Volume 37
Pages 1022-9
Authors La Cognata U, Landschutze V, Willmitzer L, Muller-Rober B
Title Structure and expression of mitochondrial citrate synthases from higher plants.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 9388613
Journal Biochem Soc Trans
Year 1997
Volume 25
Pages 380S
Authors Severcan F, Stenland C, Millhauser G
Title ESR studies of pig citrate synthase.
Related PDB
Related UniProtKB
[38]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9092828
Journal Biochemistry
Year 1997
Volume 36
Pages 3981-90
Authors Kurz LC, Roble JH, Nakra T, Drysdale GR, Buzan JM, Schwartz B, Drueckhammer DG
Title Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog.
Related PDB 1al6 1amz
Related UniProtKB
[39]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 97400454
PubMed ID 9254593
Journal Biochemistry
Year 1997
Volume 36
Pages 9983-94
Authors Russell RJ, Ferguson JM, Hough DW, Danson MJ, Taylor GL
Title The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,.
Related PDB 1aj8
Related UniProtKB Q53554
[40]
Resource
Comments
Medline ID
PubMed ID 9757123
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 1012-3
Authors Gerike U, Russell RJ, Danson MJ, Russell NJ, Hough DW, Taylor GL
Title Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 9657685
Journal Biochemistry
Year 1998
Volume 37
Pages 9724-37
Authors Kurz LC, Nakra T, Stein R, Plungkhen W, Riley M, Hsu F, Drysdale GR
Title Effects of changes in three catalytic residues on the relative stabilities of some of the intermediates and transition states in the citrate synthase reaction.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 10387046
Journal Biochemistry
Year 1999
Volume 38
Pages 8022-31
Authors Gu Z, Drueckhammer DG, Kurz L, Liu K, Martin DP, McDermott A
Title Solid state NMR studies of hydrogen bonding in a citrate synthase inhibitor complex.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 9893982
Journal Biochemistry
Year 1999
Volume 38
Pages 881-9
Authors Shatalin K, Lebreton S, Rault-Leonardon M, Velot C, Srere PA
Title Electrostatic channeling of oxaloacetate in a fusion protein of porcine citrate synthase and porcine mitochondrial malate dehydrogenase.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 9933583
Journal J Biol Chem
Year 1999
Volume 274
Pages 3941-5
Authors Haggie PM, Brindle KM
Title Mitochondrial citrate synthase is immobilized in vivo.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 10694395
Journal Biochemistry
Year 2000
Volume 39
Pages 2283-96
Authors Kurz LC, Drysdale G, Riley M, Tomar MA, Chen J, Russell RJ, Danson MJ
Title Kinetics and mechanism of the citrate synthase from the thermophilic archaeon Thermoplasma acidophilum.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 11501994
Journal J Mol Biol
Year 2001
Volume 310
Pages 1039-53
Authors Roccatano D, Mark AE, Hayward S
Title Investigation of the mechanism of domain closure in citrate synthase by molecular dynamics simulation.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 11707611
Journal Protein Eng
Year 2001
Volume 14
Pages 655-61
Authors Gerike U, Danson MJ, Hough DW
Title Cold-active citrate synthase: mutagenesis of active-site residues.
Related PDB
Related UniProtKB

Comments
This enzyme catalyzes the following reactions sequentially:
(A) Isomerization (enolization)
(B) Condensation (Addition)
(C) Hydrolysis of thioester group

Created Updated
2004-06-01 2009-02-26