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22.3 - 24.2
3,3-thiodipropionate
22.3 - 24.2
3,3-thiodipropionic acid
21.2 - 71.7
3-phosphonopropionic acid
21.2 - 71.7
3-phosphopropionate
73 - 90.5
Dihydroxyfumarate
73 - 90.5
dihydroxyfumaric acid
8 - 14.6
potassium hydroxycitrate
22.3
3,3-thiodipropionate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
24.2
3,3-thiodipropionate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
22.3
3,3-thiodipropionic acid
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
24.2
3,3-thiodipropionic acid
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
21.2
3-phosphonopropionic acid
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
71.7
3-phosphonopropionic acid
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
21.2
3-phosphopropionate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
71.7
3-phosphopropionate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
73
Dihydroxyfumarate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
90.5
Dihydroxyfumarate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
73
dihydroxyfumaric acid
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
90.5
dihydroxyfumaric acid
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
6.5
DL-malate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
14.2
DL-malate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
6.5
DL-malic acid
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
14.2
DL-malic acid
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
17.5
Maleate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
20
Maleate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
17.5
Maleic acid
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
20
Maleic acid
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
8
potassium hydroxycitrate
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
8
potassium hydroxycitrate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
14.6
potassium hydroxycitrate
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
14.6
potassium hydroxycitrate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
25.1
propionate
pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA
25.1
propionate
substrate acetyl-CoA, pH 8.0, temperature not specified in the publication
28.1
propionate
pH 8.0, temperature not specified in the publication, substrate: oxaloacetate
28.1
propionate
substrate oxaloacetate, pH 8.0, temperature not specified in the publication
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malfunction
-
citrate synthase activity reduction leads to a strong L-lysine accumulation
metabolism
-
citrate synthase is a key enzyme of the citric acid cycle that provides energy for cellular function. Additionally, the enzyme plays a critical role in providing citrate derived acetyl-CoA for lipogenesis and cholesterologenesis
metabolism
-
citrate synthase is a key enzyme of the citric acid cycle that provides energy for cellular function. Additionally, the enzyme plays a critical role in providing citrate derived acetyl-CoA for lipogenesis and cholesterologenesis
metabolism
-
the enzyme is required for both tricarboxylic acid and glyoxylic acid cycle activity
metabolism
-
Clostridium thermocellum carries both Re- and Si-citrate synthases, i.e. EC 2.3.3.3 and EC 2.3.3.1, respectively, to initiate the tricarboxic acid cycle
physiological function
-
the citrate synthase gene is a direct retinoic acid receptor-related orphan receptor alpha target and one mechanism by which retinoic acid receptor-related orphan receptor alpha regulates lipid metabolism is via regulation of citrate synthase expression
physiological function
-
the citrate synthase gene is a direct retinoic acid receptor-related orphan receptor alpha target and one mechanism by which retinoic acid receptor-related orphan receptor alpha regulates lipid metabolism is via regulation of citrate synthase expression
physiological function
during high-fat diet feeding, glucose tolerance of mice decreases progressively and to a greater extent in females with low citrate synthase activity compared to wild-type females, with males showing a similar trend. Body weight and fat gain does not differ between low CS activity and wild-type mice. After an 18 h incubation in 0.8 mM palmitate, C2C12 muscle cells with about 50% shRNA-mediated reduction in CS activity show lower viability and increased levels of cleaved caspase-3 compared to the scramble shRNA treated C2C12 cells
additional information
sequences and structures of citrate synthases from the psychrophile antarctic bacterium DS2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
additional information
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
additional information
-
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
additional information
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
additional information
-
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
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tetramer
-
2 * 45000 + 2 * 80000, alpha, beta, SDS-PAGE
dimer
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile. In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
monomer
sequences and structures of citrate synthases from the psychrophile antarctic bacterium DS2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
monomer
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility
additional information
-
in presence of nardilysin, EC 3.4.24.61, citrate synthase co-immunoprecipitates with mitochondrial malate dehydrogenase. In addition, citrate synthase binds to immobilized nardilysin
additional information
-
molecular basis of subunit interactions
additional information
-
detection of peptides within the enzyme which show strong binding with small heat shock proteins. Thermostabilization of thermosensitive citrate synthase by small heat shock proteins is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in the thermostable forms of the enzymes dimer
additional information
detection of peptides within the enzyme which show strong binding with small heat shock proteins. Thermostabilization of thermosensitive citrate synthase by small heat shock proteins is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in the thermostable forms of the enzymes dimer
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Jeffery, D.; Goodenough, P.W.; Weitzman, P.D.J.
Citrate synthase and malate dehydrogenase from tomato fruit
Phytochemistry
27
41-44
1988
Solanum lycopersicum
-
brenda
Kurz, L.C.; Shah, S.; Frieden, C.; Nakra, T.; Stein, R.E.; Drysdale, G.R.; Evans, C.T.; Srere, P.A.
Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site
Biochemistry
34
13278-13288
1995
Sus scrofa
brenda
Takahashi, R.; Usui, K.; Sakuraba, T.; Tokuyama, T.
Purification and some properties of citrate synthase from a nitrite-oxidising chemoautotroph, Nitrobacter agilis ATCC 14123
J. Ferment. Bioeng.
77
97-99
1994
Nitrobacter winogradskyi
-
brenda
Morgunov, I.G.; Sharishev, A.A.; Mikulinskaya, O.V.; Sokolov, D.M.; Finogenova, T.V.
Isolation, purification and some properties of citrate synthase from citric acid-accumulating yeasts Yarrowia (Candida) lipolytica
Biokhimiya
59
1320-1329
1994
Yarrowia lipolytica
-
brenda
Kelly, S.M.; Price, N.C.
Reactivation of denatured citrate synthase
Int. J. Biochem.
24
627-630
1992
Sus scrofa
brenda
Sylven, C.; Kallner, A.; Jansson, F.
Regional distribution of citrate synthase and lactate dehydrogenase isoenzymes in the bovine heart
Acta Physiol. Scand.
136
331-337
1989
Bos taurus
brenda
Ullian, M.E.; Robinson, C.J.; Evans, C.T.; Melnick, J.Z.; Fitzgibbon, W.R.
Role of citrate synthase in aldosterone-mediated sodium reabsorption
Hypertension
35
875-879
2000
Rattus norvegicus
brenda
Winger, Q.A.; Hill, J.R.; Watson, A.J.; Westhusin, M.E.
Characterization of a bovine cDNA encoding citrate synthase, and presence of citrate synthase mRNA during bovine pre-attachment development
Mol. Reprod. Dev.
55
14-19
2000
Bos taurus
brenda
Leek, B.T.; Mudaliar, S.R.; Henry, R.; Mathieu-Costello, O.; Richardson, R.S.
Effect of acute exercise on citrate synthase activity in untrained and trained human skeletal muscle
Am. J. Physiol.
280
R441-447
2001
Homo sapiens
brenda
Schlichtholz, B.; Turyn, J.; Goyke, E.; Biernacki, M.; Jaskiewicz, K.; Sledzinski, Z.; Swierczynski, J.
Enhanced citrate synthase activity in human pancreatic cancer
Pancreas
30
99-104
2005
Homo sapiens
brenda
Chow, K.M.; Ma, Z.; Cai, J.; Pierce, W.M.; Hersh, L.B.
Nardilysin facilitates complex formation between mitochondrial malate dehydrogenase and citrate synthase
Biochim. Biophys. Acta
1723
292-301
2005
Rattus norvegicus
brenda
Ahrman, E.; Gustavsson, N.; Hultschig, C.; Boelens, W.C.; Emanuelsson, C.S.
Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase
Extremophiles
11
659-666
2007
Sus scrofa, Sus scrofa (P00889)
brenda
Mishra, R.; Seckler, R.; Bhat, R.
Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: how well are protein folding and stability aspects coupled?
J. Biol. Chem.
280
15553-15560
2005
Sus scrofa
brenda
van der Kamp, M.W.; Perruccio, F.; Mulholland, A.J.
High-level QM/MM modelling predicts an arginine as the acid in the condensation reaction catalysed by citrate synthase
Chem. Commun. (Camb. )
2008
1874-1876
2008
Gallus gallus
brenda
da Silva Pimenta, A.; Lambertucci, R.H.; Gorjao, R.; Dos Reis Silveira, L.; Curi, R.
Effect of a single session of electrical stimulation on activity and expression of citrate synthase and antioxidant enzymes in rat soleus muscle
Eur. J. Appl. Physiol.
102
119-126
2007
Rattus norvegicus
brenda
Kohn, T.A.; Myburgh, K.H.
Regional specialization of rat quadriceps myosin heavy chain isoforms occurring in distal to proximal parts of middle and deep regions is not mirrored by citrate synthase activity
J. Anat.
210
8-18
2007
Rattus norvegicus
brenda
Beard, D.A.; Vinnakota, K.C.; Wu, F.
Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase
PLoS ONE
3
e1825
2008
Bos taurus, Rattus norvegicus
brenda
Correa, C.; Amboni, G.; Assis, L.C.; Martins, M.R.; Kapczinski, F.; Streck, E.L.; Quevedo, J.
Effects of lithium and valproate on hippocampus citrate synthase activity in an animal model of mania
Prog. Neuropsychopharmacol. Biol. Psychiatry
31
887-891
2007
Rattus norvegicus
brenda
Zanatta, A.; Schuck, P.F.; Viegas, C.M.; Knebel, L.A.; Busanello, E.N.; Moura, A.P.; Wajner, M.
In vitro evidence that D-serine disturbs the citric acid cycle through inhibition of citrate synthase activity in rat cerebral cortex
Brain Res.
1298
186-193
2009
Rattus norvegicus
brenda
Cheng, T.L.; Liao, C.C.; Tsai, W.H.; Lin, C.C.; Yeh, C.W.; Teng, C.F.; Chang, W.T.
Identification and characterization of the mitochondrial targeting sequence and mechanism in human citrate synthase
J. Cell. Biochem.
107
1002-1015
2009
Homo sapiens, Homo sapiens (O75390)
brenda
Weina, G.; Yue, M.; Xie, B.; Wan, F.; Guo, J.
Inhibition of citrate synthase thermal aggregation in vitro by recombinant small heat shock proteins
J. Microbiol. Biotechnol.
19
1628-1634
2009
Sus scrofa
brenda
Freitas, T.P.; Rezin, G.T.; Goncalves, C.L.; Jeremias, G.C.; Gomes, L.M.; Scaini, G.; Teodorak, B.P.; Valvassori, S.S.; Quevedo, J.; Streck, E.L.
Evaluation of citrate synthase activity in brain of rats submitted to an animal model of mania induced by ouabain
Mol. Cell. Biochem.
341
245-249
2010
Rattus norvegicus
brenda
Agostinho, F.R.; Reus, G.Z.; Stringari, R.B.; Ribeiro, K.F.; Ferraro, A.K.; Benedet, J.; Rochi, N.; Scaini, G.; Streck, E.L.; Quevedo, J.
Treatment with olanzapine, fluoxetine and olanzapine/fluoxetine alters citrate synthase activity in rat brain
Neurosci. Lett.
487
278-281
2011
Rattus norvegicus
brenda
Crumbley, C.; Wang, Y.; Banerjee, S.; Burris, T.P.
Regulation of expression of citrate synthase by the retinoic acid receptor-related orphan receptor alpha (RORalpha)
PLoS ONE
7
e33804
2012
Homo sapiens, Mus musculus
brenda
Kim, M.; Le, H.M.; Xie, X.; Feng, X.; Tang, Y.J.; Mouttaki, H.; McInerney, M.J.; Buckel, W.
Two pathways for glutamate biosynthesis in the syntrophic bacterium Syntrophus aciditrophicus
Appl. Environ. Microbiol.
81
8434-8444
2015
no activity in Syntrophus aciditrophicus
brenda
Kim, M.; Le, H.; McInerney, M.J.; Buckel, W.
Identification and characterization of re-citrate synthase in Syntrophus aciditrophicus
J. Bacteriol.
195
1689-1696
2013
no activity in Syntrophus aciditrophicus
brenda
Kumar, S.; Nussinov, R.
Different roles of electrostatics in heat and in cold Adaptation by citrate synthase
ChemBioChem
5
280-290
2004
antarctic bacterium DS2-3R (O34002), Gallus gallus (P23007), Gallus gallus, Pyrococcus furiosus (Q53554), Pyrococcus furiosus
brenda
Schlachter, C.R.; Klapper, V.; Radford, T.; Chruszcz, M.
Comparative studies of Aspergillus fumigatus 2-methylcitrate synthase and human citrate synthase
Biol. Chem.
400
1567-1581
2019
Homo sapiens (O75390), Homo sapiens
brenda
Xiong, W.; Lo, J.; Chou, K.; Wu, C.; Magnusson, L.; Dong, T.; Maness, P.
Isotope-assisted metabolite analysis sheds light on central carbon metabolism of a model cellulolytic bacterium Clostridium thermocellum
Front. Microbiol.
9
1947
2018
Acetivibrio thermocellus
brenda
Alhindi, Y.; Vaanholt, L.M.; Al-Tarrah, M.; Gray, S.R.; Speakman, J.R.; Hambly, C.; Alanazi, B.S.; Gabriel, B.M.; Lionikas, A.; Ratkevicius, A.
Low citrate synthase activity is associated with glucose intolerance and lipotoxicity
J. Nutr. Metab.
2019
8594825
2019
Mus musculus (Q9CZU6), Mus musculus
brenda