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AMP + diphosphate + acetyl adenylate
?
-
-
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
ATP + acetate + citrate (pro-3S)-lyase (thiol form)
AMP + diphosphate + citrate(pro-3S)-lyase (acetyl form)
-
-
-
?
ATP + acetate + citrate lyase
AMP + diphosphate + acetyl-[citrate lyase]
ATP + propionate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, propionate at 47% of the activity relative to acetate
-
-
?
CTP + acetate + citrate (pro-3S)-lyase
CMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, CTP at 30% of the relative to ATP
-
-
?
dATP + acetate + citrate (pro-3S)-lyase
dAMP + diphosphate + citrate(pro-3S)-lyase
dTTP + acetate + citrate (pro-3S)-lyase
dTMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, dTTP at 5% of the activity relative to ATP
-
-
?
GTP + acetate + citrate (pro-3S)-lyase
GMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, GTP at 43% of the activity of ATP
-
-
?
ITP + acetate + citrate (pro-3S)-lyase
IMP + diphosphate + citrate(pro-3S)-lyase
UTP + acetate + citrate (pro-3S)-lyase
UMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, UTP at 18% of the activity relative to ATP
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
?
-
thiol form of (pro-3S)-lyase, enzyme converts the inactive thiol form of EC 4.1.3.6 into the active form. EC 4.1.3.6 is the enzyme responsible for the anaerobic utilization of citrate
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
?
-
thiol form of (pro-3S)-lyase, enzyme converts the inactive thiol form of EC 4.1.3.6 into the active form. EC 4.1.3.6 is the enzyme responsible for the anaerobic utilization of citrate
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
?
-
thiol form of (pro-3S)-lyase, enzyme converts the inactive thiol form of EC 4.1.3.6 into the active form. EC 4.1.3.6 is the enzyme responsible for the anaerobic utilization of citrate
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
acetate and ATP can be replaced by acetyl adenylate
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
acetyl form
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
acetyl form
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
no acetylation of the HS-lyase from Rhodopseudomonas gelatinosa and Klebsiella aerogenes
acetyl form
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
Leuconostoc citrovorum
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
highly specific, cannot react with citrate lyases from nonphototrophic microorganisms, e.g. Enterobacter aerogenes, Clostridium sphenoides or Streptococcus diacetilactis
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
-
-
?
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase
-
-
?
ATP + acetate + citrate lyase
AMP + diphosphate + acetyl-[citrate lyase]
-
-
-
-
?
ATP + acetate + citrate lyase
AMP + diphosphate + acetyl-[citrate lyase]
-
-
-
-
?
dATP + acetate + citrate (pro-3S)-lyase
dAMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, dATP at 72% of the activity relative to ATP
-
-
?
dATP + acetate + citrate (pro-3S)-lyase
dAMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, dATP at 72% of the activity relative to ATP
-
-
?
ITP + acetate + citrate (pro-3S)-lyase
IMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, ITP at 33% of the activity relative to ATP
-
-
?
ITP + acetate + citrate (pro-3S)-lyase
IMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, ITP at 33% of the activity relative to ATP
-
-
?
ITP + acetate + citrate (pro-3S)-lyase
IMP + diphosphate + citrate(pro-3S)-lyase
-
thiol form of (pro-3S)-lyase, ITP at 46% of the activity relative to ATP
-
-
?
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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
Lactococcus lactis subsp. lactis, Leuconostoc citrovorum
brenda
Antranikian, G.; Gottschalk, G.
Phosphorylation of citrate lyase ligase in Clostridium sphenoides and regulation of anaerobic citrate metabolism in other bacteria
Biochimie
71
1029-1037
1989
Lacrimispora sphenoides
brenda
Antranikian, G.; Herzberg, C.; Gottschalk, G.
Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation
Eur. J. Biochem.
153
413-420
1985
Lacrimispora sphenoides, [Clostridium] sporosphaeroides, Lactococcus lactis, Lacrimispora sphenoides C2 / DSM 614
brenda
Schmellenkamp, H.; Eggerer, H.
Mechanism of enzymic acetylation of des-acetyl citrate lyase
Proc. Natl. Acad. Sci. USA
71
1987-1991
1974
Klebsiella aerogenes
brenda
Antranikian, G.; Gottschalk, G.
Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes
Eur. J. Biochem.
126
43-47
1982
Rubrivivax gelatinosus
brenda
Quentmeier, A.; Antranikian, G.
Characterization of citrate lyase from Clostridium sporosphaeroides
Arch. Microbiol.
141
85-90
1985
[Clostridium] sporosphaeroides
brenda
Antranikian, G.; Giffhorn, F.; Gottschalk, G.
Activation and inactivation of citrate lyase ligase from Rhodopseudomonas gelatinosa
FEBS Lett.
88
67-70
1978
Rubrivivax gelatinosus
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
Martin, M.; Corrales, M.A.; de Mendoza, D.; Lopez, P.; Magni, C.
Cloning and molecular characterization of the citrate utilization citMCDEFGRP cluster of Leuconostoc paramesenteroides
FEMS Microbiol. Lett.
174
231-238
1999
Weissella paramesenteroides
brenda