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EC Tree
IUBMB Comments In the proteobacterium Rubrivivax gelatinosus, this enzyme modulates the activity of EC 4.1.3.6, citrate (pro-3S)-lyase, by converting it from its active acetyl form into its inactive thiol form by removal of its acetyl groups . The activity of citrate-lyase deacetylase is itself inhibited by L-glutamate .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
citrate lyase deacetylase, acetyl-s-(acyl-carrier protein) enzyme thioester hydrolase (acetate),
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acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase (acetate)
citrate lyase deacetylase
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[citrate-(pro-3S)-lyase] thiolesterase
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acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase (acetate)
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acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase (acetate)
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acetyl-[citrate (pro-3S)-lyase] + H2O = holo-[citrate (pro-3S)-lyase] + acetate
hydrolysis inactivates EC 4.1.3.6 citrate (pro-3S)-lyase
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hydrolysis of thioester
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[citrate-(pro-3S)-lyase](acetyl-form) hydrolase
In the proteobacterium Rubrivivax gelatinosus, this enzyme modulates the activity of EC 4.1.3.6, citrate (pro-3S)-lyase, by converting it from its active acetyl form into its inactive thiol form by removal of its acetyl groups [2]. The activity of citrate-lyase deacetylase is itself inhibited by L-glutamate [2].
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
additional information
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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regulates the activity of citrate layse by covalent modification
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additional information
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purified citrate lyases from Enterobacter aerogenes, Streptococcus diacetilactis and Clostridium sphenoides are no substrates
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additional information
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acetyl-CoA, acetoacetyl-CoA, S-acetyl-N-acetylcyseamine and purified citrate lyases from Enterobacter aerogenes and Streptococcus diacetilactis are no substrates, reaction with butyryl-S-citrate lyase, propionyl-S-citrate lyaseand acetyl-S-citrate lyase only slightly faster than spontaneous hydrolysis
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
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regulates the activity of citrate layse by covalent modification
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alpha-glutamyl-glutamate
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10 mM, 70% inhibition
D-glutamate
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10 mM, 54% inhibition
EDTA
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0.01 M, 40% inhibition
gamma-glutamyl-glutamate
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10 mM, 70% inhibition
L-arginine
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0.01 M, 47% inhibition
L-aspartate
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L-aspartate
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10 mM, 60% inhibition
L-glutamate
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L-glutamate
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linear mixed type of inhibition
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antibodies against the large subunit of citrate lyase inhibits the deacetylase, antibodies against the middle and small subunits does not
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D-glutamate, 2-oxoglutarate, L-alpha-hydroxyglutarate and L-proline are less effective inhibitors, iodoacetate, iodoacetamide or N-ethylmaleimide does not interfere with deacetylase activity
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additional information
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0.0001
[citrate (pro-3S)-lyase](acetyl form)
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pH 7.2, 30°C
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0.12
L-glutamate
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pH 7.5, 30°C
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additional information
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specific activity 1000 U/mg
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specific activity 15.00 U/mg
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no activity in Clostridium sphenoides
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no activity in Enterobacter aerogenes
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no activity in Escherichia coli
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no activity in Streptococcus diacetilactis
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DSM 149
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7300
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2 * 7300, SDS-PAGE
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dimer
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2 * 7300, SDS-PAGE
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7.2 - 8.1
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because of the instability of the substrate acetyl-S-citrate lyase at acidic and alkaline pH-values, all assays are carried out at pH 7.2, where the spontanous hydrolysis of the substrate is negligible and the enzyme shows 70% of the activity at pH 8.1
643850
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50
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half-life 20 min, effectively protected against heat inactivation by 100 mM L-glutamate, half-life 30 min
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loses activity upon repeated freezing and thawing
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-15°C, purified enzyme stable for at least 6 months
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-20°C, partly purified enzyme retains full activity for at least 1 year
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-20°C, purified enzyme loses 20% of activity within 1 year during storage
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Giffhorn, F.; Gottschalk, G.
Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+)-glutamate
J. Bacteriol.
124
1052-1061
1975
no activity in Enterobacter aerogenes, no activity in Streptococcus diacetilactis, Rubrivivax gelatinosus
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Giffhorn, F.; Rode, H.; Kuhn, A.; Gottschalk, G.
Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate
Eur. J. Biochem.
111
461-471
1980
no activity in Enterobacter aerogenes, no activity in Escherichia coli, no activity in Streptococcus diacetilactis, Rubrivivax gelatinosus
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Giffhorn, F.; Zimmermann, T.; Kuhn, A.
Substrate specificity of citrate lyase deacetylase of Rhodopseudomonas gelatinosa and Rhodopseudomonas palustris
J. Bacteriol.
147
463-470
1981
no activity in Clostridium sphenoides, Rhodopseudomonas palustris, Rubrivivax gelatinosus
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3.1.2.16 citrate-lyase deacetylase
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