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Ca2+
required, addition of citrate before Ca2+ initially results in acidification of the cytoplasm, the Ca2+-citrate metabolic pathway as a whole does not produce a net proton electrochemical gradient
Cu2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Co2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+
Co2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Fe2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
-
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+. Mg2+ and Mn2+ are most effective
Mg2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+. Mg2+ and Mn2+ are most effective
Mg2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+. Mg2+ is most effective
Mg2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+, Mg2+ is most effective
Mn2+
-
-
Mn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
cooperative, binding of Mn2+ involves a conformational change in the enzyme complex
Mn2+
-
Mg2+ and Mn2+ are most effective divalent metal ions
Mn2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+
Mn2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Zn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
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10000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
10427
-
alpha6beta6gamma6, 6 * 10427, gamma, + 6 * 31352, beta, + 6 * 54668, alpha, calculation from nucleotide sequence
11000
-
x * 11000 + x * 32000 + x * 54500, gel filtration in presence of 6 M guanidinium chloride
11700
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
11800
-
x * 11800, + x * 34000 + x * 56600, SDS-PAGE
11900
-
x * 11900 + x * 33800 + x * 55800, SDS-PAGE
12000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
30000
-
x * 30000 + x * 61000, SDS-PAGE
31352
-
alpha6beta6gamma6, 6 * 10427, gamma, + 6 * 31352, beta, + 6 * 54668, alpha, calculation from nucleotide sequence
31600
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
33000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
33800
-
x * 11900 + x * 33800 + x * 55800, SDS-PAGE
35000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
37000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
44600
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
515000
-
gel filtration, sucrose density gradient centrifugation
520000
-
equilibrium sedimentation
530000
-
equilibrium sedimentation
536600
-
gel filtration, sedimentation equilibrium centrifugation
54500
-
x * 11000 + x * 32000 + x * 54500, gel filtration in presence of 6 M guanidinium chloride
54668
-
alpha6beta6gamma6, 6 * 10427, gamma, + 6 * 31352, beta, + 6 * 54668, alpha, calculation from nucleotide sequence
550000
-
meniscus depletion equilibrium sedimentation
55800
-
x * 11900 + x * 33800 + x * 55800, SDS-PAGE
56000
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
56600
-
x * 11800, + x * 34000 + x * 56600, SDS-PAGE
580000
-
disc gel electrophoresis
61000
-
x * 30000 + x * 61000, SDS-PAGE
11760
-
apo-ACP-His, mass spectrometry
11760
-
apo-ACP-His, mass spectrometry
12500
-
apo-ACP-His, SDS-PAGE
12500
-
apo-ACP-His, SDS-PAGE
12650
-
holo-ACP-His, mass spectrometry
12650
-
holo-ACP-His, mass spectrometry
14000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
14000
-
x * 14000 + x * 34000 + x * 55000, SDS-PAGE
15000
-
holo-ACP-His, SDS-PAGE
15000
-
holo-ACP-His, SDS-PAGE
32000
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
32000
-
alpha6beta6gamma, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000,acyl-carrier-protein gamma-subunit, SDS-PAGE
32000
-
x + 10000, + x * 32000, + x * 54000, SDS-PAGE
32000
-
x * 11000 + x * 32000 + x * 54500, gel filtration in presence of 6 M guanidinium chloride
34000
-
x * 14000 + x * 34000 + x * 55000, SDS-PAGE
34000
-
x * 11800, + x * 34000 + x * 56600, SDS-PAGE
54000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
54000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
54000
-
alpha6beta6gamma, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000,acyl-carrier-protein gamma-subunit, SDS-PAGE
54000
-
x + 10000, + x * 32000, + x * 54000, SDS-PAGE
55000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
55000
-
x * 14000 + x * 34000 + x * 55000, SDS-PAGE
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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oligomer
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
oligomer
-
alpha6beta6gamma, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000,acyl-carrier-protein gamma-subunit, SDS-PAGE
oligomer
-
x + 10000, + x * 32000, + x * 54000, SDS-PAGE
oligomer
-
alpha6beta6gamma6, 6 * 10427, gamma, + 6 * 31352, beta, + 6 * 54668, alpha, calculation from nucleotide sequence
oligomer
-
x * 11900 + x * 33800 + x * 55800, SDS-PAGE
oligomer
-
x * 11000 + x * 32000 + x * 54500, gel filtration in presence of 6 M guanidinium chloride
oligomer
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
oligomer
-
x * 14000 + x * 34000 + x * 55000, SDS-PAGE
oligomer
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
oligomer
-
x * 30000 + x * 61000, SDS-PAGE
oligomer
-
x * 11800, + x * 34000 + x * 56600, SDS-PAGE
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
-
the presence of ethanol, in a concentration range from 2% to 8%, induces a gradual increase in enzyme activity. The enzyme expression is induced in the presence of citric acid, acetic acid, and lactic acid. The enzyme is optimally produced when bacteria are grown below pH 4.0 and at 35-40C
-
-
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Kummel, A.; Behrens, G.; Gottschalk, G.
Citrate lyase from Streptococcus diacetilactis. Association with its acetylating enzyme
Arch. Microbiol.
102
111-116
1975
Klebsiella pneumoniae, Lactococcus lactis subsp. lactis, Leuconostoc citrovorum, Rubrivivax gelatinosus
brenda
Quentmeier, A.; Antranikian, G.
Characterization of citrate lyase from Clostridium sporosphaeroides
Arch. Microbiol.
141
85-90
1985
[Clostridium] sporosphaeroides
brenda
Bekal, S.; van Beeumen, J.; Samyn, B.; Garmyn, D.; Henini, S.; Divies, C.; Prevost, H.
Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster
J. Bacteriol.
180
647-654
1998
Leuconostoc mesenteroides
brenda
Bekal, S.; Divies, C.; Prevost, H.
Citrate lyases of lactic acid bacteria
Lait
78
3-10
1998
Leuconostoc mesenteroides, Lacrimispora sphenoides, Escherichia coli, Enterococcus faecalis, Klebsiella pneumoniae, Lactococcus lactis subsp. lactis, Lactococcus lactis, Rubrivivax gelatinosus, Lactococcus lactis subsp. diacetylactis
-
brenda
Bowen, T.J.; Mortimer, M.G.
Sub-units of citrate oxaloacetate-lyase
Eur. J. Biochem.
23
262-266
1971
Klebsiella pneumoniae
brenda
Srere, P.A.; Boettger, B.; Brooks, G.C.
Citrate lyase: a pantothenate-containing enzyme
Proc. Natl. Acad. Sci. USA
69
1201-1202
1972
Klebsiella pneumoniae
brenda
Spector, L.B.
Citrate cleavage and related enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
357-389
1972
Escherichia coli, Enterococcus faecalis, Klebsiella pneumoniae, Lactococcus lactis subsp. lactis
-
brenda
Singh, M.; Carpenter, D.E.; Srere, P.A.
Nonidentical subunits of citrate lyase from Klebsiella aerogenes
Biochem. Biophys. Res. Commun.
59
1211-1218
1974
Klebsiella pneumoniae
brenda
Beuscher, N.; Mayer, F.; Gottschalk, G.
Citrate lyase from Rhodopseudomonas gelatinosa: purification, electron microscopy and subunit structure
Arch. Microbiol.
100
307-328
1974
Rubrivivax gelatinosus
brenda
Carpenter, D.E.; Singh, M.; Richards, E.G.; Srere, P.A.
On the molecular weights of the three nonidentical subunits of citrate lyase from Klebsiella aerogenes
J. Biol. Chem.
250
3254-3260
1975
Klebsiella pneumoniae
brenda
Hiremath, S.T.; Paranjpe, S.; SivaRaman, C.
Purification and properties of citrate lyase from Streptococcus faecalis
Biochem. Biophys. Res. Commun.
72
1122-1128
1976
Enterococcus faecalis
brenda
Srere, P.A.
The enzymology of the formation and breakdown of citrate
Adv. Enzymol. Relat. Areas Mol. Biol.
43
57-101
1975
Klebsiella pneumoniae, Lactococcus lactis subsp. lactis
brenda
Giffhorn, F.; Gottschalk, G.
Crystallization and subunit composition of citrate lyase of Rhodopseudomonas gelatinosa
FEBS Lett.
96
175-178
1978
Rubrivivax gelatinosus
brenda
Sivaraman, H.; Sivaraman, C.
Cooperative binding of manganese to citrate lyase from Klebsiella aerogenes
FEBS Lett.
105
267-270
1979
Klebsiella pneumoniae
brenda
Antranikian, G.; Klinner, C.; Kuemmel, A.; Schwanitz, D.; Zimmermann, T.; Mayer, F.; Gottschalk, G.
Purification of L-glutamate-dependent citrate lyase from Clostridium sphenoides and electron microscopic analysis of citrate lyase isolated from Rhodopseudomonas gelatinosa, Streptococcus diacetilactis and C. sphenoides
Eur. J. Biochem.
126
35-42
1982
Lacrimispora sphenoides, Lactococcus lactis subsp. lactis, Rubrivivax gelatinosus
brenda
Subramanian, S.; Sivaraman, C.
Bacterial citrate lyase
J. Biosci.
6
379-401
1984
Enterobacter cloacae, Aerobacter indologenes, [Clostridium] symbiosum, Lacrimispora indolis, Fusobacterium mortiferum, Lacrimispora sphenoides, Clostridium sporogenes, [Clostridium] sporosphaeroides, Clostridium subterminale, Escherichia coli, Enterococcus faecalis, Klebsiella pneumoniae, Lactococcus lactis subsp. lactis, Leuconostoc citrovorum, no activity in Chlorobium thiosulfatophilum, no activity in Rhodospirillum rubrum, Providencia rettgeri, Rubrivivax gelatinosus, Rhodopseudomonas palustris, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Nilekani, S.; SivaRaman, C.
Purification and properties of citrate lyase from Escherichia coli
Biochemistry
22
4657-4663
1983
Escherichia coli
brenda
Matsumoto, K.; Tsukatani, T.
Simultaneous quantitation of citrate and isocitrate in citrus juice by a flow-injection method based on the use of enzyme reactors
Anal. Chim. Acta
321
157-164
1996
Klebsiella pneumoniae
-
brenda
David, P.F.; Boquien, C.Y.; Nakache, F.; Bassit, N.; Hartley, D.; Paraf, A.; Corrieu, G.
Quantification of citrate lyase by enzyme-linked immunosorbent assay for determining the population of Lactococcus lactis subsp. lactis biovar diacetilactis in pure and mixed cultures
Appl. Microbiol. Biotechnol.
44
68-74
1995
Lactococcus lactis
-
brenda
Dimroth, P.; Eggerer, H.
Isolation of subunits of citrate lyase and characterization of their function in the enzyme complex
Proc. Natl. Acad. Sci. USA
72
3458-3462
1975
Klebsiella pneumoniae
brenda
Bott, M.; Dimroth, P.
Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression
Mol. Microbiol.
14
347-356
1994
Klebsiella pneumoniae
brenda
Petrarulo, M.; Facchini, P.; Cerelli, E.; Marangella, M.; Linari, F.
Citrate in urine determined with a new citrate lyase method
Clin. Chem.
41
1518-1521
1995
Klebsiella pneumoniae
brenda
Schneider, K.; Dimroth, P.; Bott, M.
Biosynthesis of the prosthetic group of citrate lyase
Biochemistry
39
9438-9450
2000
Escherichia coli, Klebsiella pneumoniae
brenda
Schneider, K.; Kastner, C.N.; Meyer, M.; Wessel, M.; Dimroth, P.; Bott, M.
Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group
J. Bacteriol.
184
2439-2446
2002
Klebsiella pneumoniae
brenda
Morikawa, J.; Nishimura, Y.; Uchida, A.; Tanaka, T.
Molecular cloning of novel mouse and human putative citrate lyase beta-subunit
Biochem. Biophys. Res. Commun.
289
1282-1286
2001
Homo sapiens (Q8N0X4), Mus musculus (Q8R4N0)
brenda
de Figueroa, R.M.; Oliver, G.; de Cardenas, I.L.B.
Influence of temperature on flavour compound production from citrate by Lactobacillus rhamnosus ATCC 7469
Microbiol. Res.
155
257-262
2001
Lacticaseibacillus rhamnosus
brenda
Martin, M.G.; Sender, P.D.; Peiru, S.; de Mendoza, D.; Magni, C.
Acid-inducible transcription of the operon encoding the citrate lyase complex of Lactococcus lactis biovar diacetylactis CRL264
J. Bacteriol.
186
5649-5660
2004
Lactococcus lactis
brenda
Hu, Y.; Holden, J.F.
Citric acid cycle in the hyperthermophilic archaeon Pyrobaculum islandicum grown autotrophically, heterotrophically, and mixotrophically with acetate
J. Bacteriol.
188
4350-4355
2006
Pyrobaculum islandicum
brenda
Srivastava, V.; Deshpande, S.N.; Nimgaonkar, V.L.; Lerer, B.; Thelma, B.
Genetic correlates of olanzapine-induced weight gain in schizophrenia subjects from north India: role of metabolic pathway genes
Pharmacogenomics
9
1055-1068
2008
Homo sapiens
brenda
Mortera, P.; Pudlik, A.; Magni, C.; Alarcon, S.; Lolkema, J.S.
Ca2+-citrate uptake and metabolism in Lactobacillus casei ATCC 334
Appl. Environ. Microbiol.
79
4603-4612
2013
Lacticaseibacillus casei (Q037K5), Lacticaseibacillus casei ATCC 334 (Q037K5)
brenda
Chung, C.Y.; Yam, V.W.
Induced self-assembly of platinum(II) alkynyl complexes through specific interactions between citrate and guanidinium for proof-of-principle detection of citrate and an assay of citrate lyase
Chemistry
20
13016-13027
2014
Klebsiella pneumoniae
brenda
Ouattara, H.D.; Ouattara, H.G.; Droux, M.; Reverchon, S.; Nasser, W.; Niamke, S.L.
Lactic acid bacteria involved in cocoa beans fermentation from ivory coast species diversity and citrate lyase production
Int. J. Food Microbiol.
256
11-19
2017
Leuconostoc mesenteroides, Lactiplantibacillus plantarum, Lacticaseibacillus casei, Lactiplantibacillus plantarum T11G3, Lactiplantibacillus plantarum T10AG26, Lacticaseibacillus casei T10G5, Leuconostoc mesenteroides T8AB6, Lactiplantibacillus plantarum T8N10
brenda