BRENDA - Enzyme Database show
show all sequences of 6.2.1.22

Citrate lyase from Streptococcus diacetilactis. Association with its acetylating enzyme

Kummel, A.; Behrens, G.; Gottschalk, G.; Arch. Microbiol. 102, 111-116 (1975)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + acetate + citrate (pro-3S)-lyase
Lactococcus lactis subsp. lactis
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
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactococcus lactis subsp. lactis
-
associated with citrate lyase
-
Leuconostoc citrovorum
-
associated with citrate lyase
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Leuconostoc citrovorum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + acetate + citrate (pro-3S)-lyase
thiol form of (pro-3S)-lyase
693
Leuconostoc citrovorum
AMP + diphosphate + citrate(pro-3S)-lyase
-
-
-
-
ATP + acetate + citrate (pro-3S)-lyase
thiol form of (pro-3S)-lyase
693
Lactococcus lactis subsp. lactis
AMP + diphosphate + citrate(pro-3S)-lyase
acetyl form
693
Lactococcus lactis subsp. lactis
-
ATP + acetate + citrate (pro-3S)-lyase
no acetylation of the HS-lyase from Rhodopseudomonas gelatinosa and Klebsiella aerogenes
693
Lactococcus lactis subsp. lactis
AMP + diphosphate + citrate(pro-3S)-lyase
acetyl form
693
Lactococcus lactis subsp. lactis
-
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
693
Lactococcus lactis subsp. lactis
?
-
-
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + acetate + citrate (pro-3S)-lyase
Lactococcus lactis subsp. lactis
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
?
-
-
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Leuconostoc citrovorum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + acetate + citrate (pro-3S)-lyase
thiol form of (pro-3S)-lyase
693
Leuconostoc citrovorum
AMP + diphosphate + citrate(pro-3S)-lyase
-
-
-
-
ATP + acetate + citrate (pro-3S)-lyase
thiol form of (pro-3S)-lyase
693
Lactococcus lactis subsp. lactis
AMP + diphosphate + citrate(pro-3S)-lyase
acetyl form
693
Lactococcus lactis subsp. lactis
-
ATP + acetate + citrate (pro-3S)-lyase
no acetylation of the HS-lyase from Rhodopseudomonas gelatinosa and Klebsiella aerogenes
693
Lactococcus lactis subsp. lactis
AMP + diphosphate + citrate(pro-3S)-lyase
acetyl form
693
Lactococcus lactis subsp. lactis
-
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
693
Lactococcus lactis subsp. lactis
?
-
-
-
-
Other publictions for EC 6.2.1.22
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
651344
Martin
Cloning and molecular characte ...
Weissella paramesenteroides
FEMS Microbiol. Lett.
174
231-238
1999
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1
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33346
Bekal
Purification of Leuconostoc me ...
Leuconostoc mesenteroides
J. Bacteriol.
180
647-654
1998
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1
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7
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1
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1
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1
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1
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1
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694
Antranikian
Phosphorylation of citrate lya ...
Clostridium sphenoides
Biochimie
71
1029-1037
1989
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2
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1
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4
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1
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1
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1
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695
Antranikian
Covalent modification of citra ...
Clostridium sphenoides, Clostridium sphenoides C2 / DSM 614, Clostridium sporosphaeroides, Lactococcus lactis
Eur. J. Biochem.
153
413-420
1985
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1
1
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2
2
2
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8
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1
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1
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10
1
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1
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-
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1
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1
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2
2
2
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1
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1
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10
1
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1
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698
Quentmeier
Characterization of citrate ly ...
Clostridium sporosphaeroides
Arch. Microbiol.
141
85-90
1985
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4
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1
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1
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697
Antranikian
Copurification of citrate lyas ...
Rubrivivax gelatinosus
Eur. J. Biochem.
126
43-47
1982
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1
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3
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1
2
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4
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1
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1
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8
1
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1
1
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1
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3
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1
2
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1
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1
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8
1
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1
1
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700
Antranikian
Activation and inactivation of ...
Rubrivivax gelatinosus
FEBS Lett.
88
67-70
1978
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2
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1
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1
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693
Kummel
Citrate lyase from Streptococc ...
Lactococcus lactis subsp. lactis, Leuconostoc citrovorum
Arch. Microbiol.
102
111-116
1975
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1
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2
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1
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4
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1
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1
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4
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696
Schmellenkamp
Mechanism of enzymic acetylati ...
Klebsiella aerogenes
Proc. Natl. Acad. Sci. USA
71
1987-1991
1974
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3
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3
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1
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2
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