2.3.3.16: citrate synthase (unknown stereospecificity)
This is an abbreviated version!
For detailed information about citrate synthase (unknown stereospecificity), go to the full flat file.
Word Map on EC 2.3.3.16
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2.3.3.16
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4.1.3.7
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malate
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1.1.1.35
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glyoxysomal
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1.2.4.1
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al-induced
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agriculture
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synthesis
- 2.3.3.16
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4.1.3.7
- malate
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1.1.1.35
- glyoxysomal
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1.2.4.1
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al-induced
- agriculture
- synthesis
Reaction
Synonyms
bifunctional citrate synthase/2-methylcitrate synthase, CCNA_01983, CIT1, CitA, citrate condensing enzyme, citrate oxaloacetate-lyase (CoA-acetylating), citrate oxaloacetate-lyase, CoA-acetylating, citrate synthase, citrate synthase Cit1, citrate synthase/2-methylcitrate synthase, citrate synthetase, citric synthase, citric-condensing enzyme, citrogenase, CitZ, CS, CS1, CS2, CS3, CS4, CSI, CSY, CSY4, CTS, EC 4.1.3.7, gltA, GltA2, MCS, mitochondrial citrate synthase, mmgD, More, Msed_1522, oxalacetic transacetase, oxaloacetate transacetase, peroxisomal citrate synthase, Rv0896, SbnG, Si-citrate synthase, sll0401, SSO2589, St0589, St1805, synthase, citrate, TTHA1343, type II citrate synthase
ECTree
2.3.3.16 citrate synthase (unknown stereospecificity)Advanced search results
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results (Engineering
Engineering on EC 2.3.3.16 - citrate synthase (unknown stereospecificity)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A361R
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site-directed mutagenesis, slightly reduced kcat , reduced Km for acetyl-CoA and increased Km for oxaloacetate, enhanced activity with propionyl-CoA
A361R/A10E
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site-directed mutagenesis, reduced kcat, reduced Km for acetyl-CoA
A10E
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site-directed mutagenesis, reduced kcat, increased Km for acetyl-CoA
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A361R
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site-directed mutagenesis, slightly reduced kcat , reduced Km for acetyl-CoA and increased Km for oxaloacetate, enhanced activity with propionyl-CoA
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A361R/A10E
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site-directed mutagenesis, reduced kcat, reduced Km for acetyl-CoA
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D362A
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acetyl-CoA binding site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
G181E
the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH
H229Q
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active site mutant, reduced turnover, increased Ki for 2-oxoglutarate
H264A
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acetyl-CoA binding site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
K167A
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extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme
R109L
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extremely weak inhibition by NADH. Great structural change. Both regions - residue 260-311 and 316-342 - are much less mobile than in wild-type enzyme
R163L
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extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme
R407L
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active site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
T204R
the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH
H309G
site-directed mutagenesis, mutant allelic strain, altered developmental phenotype
D113A
D113S
D177A
the mutant shows reduced activity compared to the wild type enzyme
E151Q
the mutant shows reduced activity compared to the wild type enzyme
E46Q
the mutant shows reduced activity compared to the wild type enzyme
H47A
the mutant shows reduced activity compared to the wild type enzyme
H96A
the mutant shows reduced activity compared to the wild type enzyme
R72A
the mutant shows reduced activity compared to the wild type enzyme
D317G
D317 removes the acetyl-CoA methyl proton during catalysis
D317N
D317 removes the acetyl-CoA methyl proton during catalysis
G196V
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site-directed mutagenesis, mutation interferes with dimerization, improper dimerization or dissociation of the dimer, reduced enzyme activity and conformational stability
H187Q
H222Q
S43C
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site-directed mutagenesis, 5.7fold reduced activity, unaltered Km values for the substrates and unaltered thermostability
W245F/W115F/W17F
W348Y
additional information
D113A
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site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly increased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability
D113S
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site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly decreased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability
W348Y
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analysis of tryptophan fluorescence, residue responsible for quenching effect
additional information
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introduction of a loop into the active site of wild-type, mutant K313L, K313L/A361R/A10E , and mutant K313L/A361R, the latter showing increased thermostability and decreased temperature optimum for catalytic activity, Km and activities
additional information
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introduction of a loop into the active site of wild-type, mutant K313L, K313L/A361R/A10E , and mutant K313L/A361R, the latter showing increased thermostability and decreased temperature optimum for catalytic activity, Km and activities
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additional information
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whereas strain WTDELTAP1gltA still exhibits 15% of the activity of the wild type enzyme, no citrate synthase activity is detected in extracts of strain WTDELTAP12gltA
additional information
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construction of transgenic Arabidopsis thaliana plants ectopically overexpressing the Daucus carota citrate synthase gene via transformation with Agrobacterium tumefaciens, transgenic plants process the enzyme to its mature form, targeting into mitochondria, increased growth and phosphate accumulation
additional information
construction of transgenic Arabidopsis thaliana plants ectopically overexpressing the Daucus carota citrate synthase gene via transformation with Agrobacterium tumefaciens, transgenic plants process the enzyme to its mature form, targeting into mitochondria, increased growth and phosphate accumulation
additional information
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construction of transgenic Arabidopsis thaliana plants via Agrobacterium infection, functional expression and targeting to the mitochondria
additional information
construction of transgenic Arabidopsis thaliana plants via Agrobacterium infection, functional expression and targeting to the mitochondria
additional information
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effect of active-site mutantions on substrate binding
additional information
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knockout of citrate syntase gltA or phosphoenolpyruvate carboxylase ppc decreases the maximum cell density by 10% and 7%, resp. Over-expression of gltA or ppc increases the maximum cell dry weight by 23% and 91% resp. No acetate excretion is detected at these increased cell densities
additional information
deletion mutants, altered developmental phenotypes, complete deletion reveals that the enzyme is more important for completion of meiosis than for catalytic activity
additional information
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deletion mutants, altered developmental phenotypes, complete deletion reveals that the enzyme is more important for completion of meiosis than for catalytic activity
additional information
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overexpression of Pseudomonas aeruginosa citrate synthase in transgenic alfalfa, Medicago sativa, plants leads to increased soil aluminum tolerance and increased exclusion of Al from the root tip, overview
additional information
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construction of mutant with disrupted inter-subunit ionic network by partly eleminating the C-terminal end amino acid residues, increased Km for substrates, reduced thermostability
additional information
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construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits
additional information
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citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
additional information
citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
additional information
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citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
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additional information
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no channeling of oxaloacetate between malate dehydrogenase and citrate synthase in a recombinant fusion protein using a coupled assay
additional information
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construction of mutants with reduced enzymic activity by localized random PCR mutagenesis. In symbiosis with alfalfa, alfalfa plants form fully effective nodules when infected with Sinorhizobium meliloti mutants having as low as 7% of citrate synthase activity. Mutants with about 3% of wild-type citrate synthase activity form nodules with lower nitrogenase activity and a mutant with 0.5% of wild-type activity forms Fix-nodules
additional information
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construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits
