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 | 1aj8 1al6 | |
M-CSA | 1aj8 1al6 | |
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 15351 |
15377 15377 |
30744 30744 |
15346 15346 |
30769 30769 |
||||||||
PubChem |
444493 6302 444493 6302 |
22247451 962 22247451 962 |
970 970 |
6816 87642 6816 87642 |
19782904 311 88113319 19782904 311 88113319 |
||||||||
1aj8A01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1aj8B01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1al6A01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1amzA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1cshA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1csiA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1csrA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1cssA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
2cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
3cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
4cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
5cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
5cscB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
5ctsA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
6cscA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
6cscB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
6ctsA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1ctsA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
2ctsA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
4ctsA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
4ctsB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1aj8A02 | Unbound | Unbound | Bound:COA | Bound:CIT | Unbound | ||||||||
1aj8B02 | Unbound | Unbound | Bound:COA | Bound:CIT | Unbound | ||||||||
1al6A02 | Analogue:HAX | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
1amzA02 | Analogue:NMX | Analogue:MLT | Unbound | Unbound | Unbound | ||||||||
1cscA02 | Analogue:CMC | Analogue:MAL | Unbound | Unbound | Unbound | ||||||||
1cshA02 | Analogue:AMX | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
1csiA02 | Analogue:CMX | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
1csrA02 | Analogue:FAM | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
1cssA02 | Analogue:FCX | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
2cscA02 | Analogue:CMC | Analogue:MAL | Unbound | Unbound | Unbound | ||||||||
3cscA02 | Bound:ACO | Analogue:MAL | Unbound | Unbound | Unbound | ||||||||
4cscA02 | Bound:ACO | Analogue:MAL | Unbound | Unbound | Unbound | ||||||||
5cscA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
5cscB02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
5ctsA02 | Analogue:CMC | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
6cscA02 | Analogue:COF | Unbound | Unbound | Bound:CIT | Unbound | ||||||||
6cscB02 | Analogue:COF | Unbound | Unbound | Bound:CIT | Unbound | ||||||||
6ctsA02 | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CIC | ||||||||
1ctsA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
2ctsA02 | Unbound | Unbound | Bound:COA | Bound:CIT | Unbound | ||||||||
4ctsA02 | Unbound | Bound:OAA | Unbound | Unbound | Unbound | ||||||||
4ctsB02 | 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 | HIS 223 | |||||||||
1aj8B01 | HIS 223 | |||||||||
1al6A01 | HIS 274 | |||||||||
1amzA01 | HIS 274 | |||||||||
1cscA01 | HIS 274 | |||||||||
1cshA01 | HIS 274 | |||||||||
1csiA01 | HIS 274 | |||||||||
1csrA01 | HIS 274 | |||||||||
1cssA01 | HIS 274 | |||||||||
2cscA01 | HIS 274 | |||||||||
3cscA01 | HIS 274 | |||||||||
4cscA01 | HIS 274 | |||||||||
5cscA01 | HIS 274 | |||||||||
5cscB01 | HIS 274 | |||||||||
5ctsA01 | HIS 274 | |||||||||
6cscA01 | HIS 274 | |||||||||
6cscB01 | HIS 274 | |||||||||
6ctsA01 | HIS 274 | |||||||||
1ctsA01 | HIS 274 | |||||||||
2ctsA01 | HIS 274 | |||||||||
4ctsA01 | HIS 274 | |||||||||
4ctsB01 | HIS 274 | |||||||||
1aj8A02 | HIS 262;ASP 312 | |||||||||
1aj8B02 | HIS 262;ASP 312 | |||||||||
1al6A02 | HIS 320;ASP 375 | |||||||||
1amzA02 | HIS 320;ASP 375 | |||||||||
1cscA02 | HIS 320;ASP 375 | |||||||||
1cshA02 | HIS 320;ASP 375 | |||||||||
1csiA02 | HIS 320;ASP 375 | |||||||||
1csrA02 | HIS 320;ASP 375 | |||||||||
1cssA02 | HIS 320;ASP 375 | |||||||||
2cscA02 | HIS 320;ASP 375 | |||||||||
3cscA02 | HIS 320;ASP 375 | |||||||||
4cscA02 | HIS 320;ASP 375 | |||||||||
5cscA02 | HIS 320;ASP 375 | |||||||||
5cscB02 | HIS 320;ASP 375 | |||||||||
5ctsA02 | HIS 320;ASP 375 | |||||||||
6cscA02 | HIS 320;ASP 375 | |||||||||
6cscB02 | HIS 320;ASP 375 | |||||||||
6ctsA02 | HIS 320;ASP 375 | |||||||||
1ctsA02 | HIS 320;ASP 375 | LYS 368(N6,N6,N6-trimethyllysine) | ||||||||
2ctsA02 | HIS 320;ASP 375 | LYS 368(N6,N6,N6-trimethyllysine) | ||||||||
4ctsA02 | HIS 320;ASP 375 | LYS 368(N6,N6,N6-trimethyllysine) | ||||||||
4ctsB02 | 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. |
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. |
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. |
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, |
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, |
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. |
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, |
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, |
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 |