Information on EC 6.2.1.22 - [citrate (pro-3S)-lyase] ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.22
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RECOMMENDED NAME
GeneOntology No.
[citrate (pro-3S)-lyase] ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + [citrate (pro-3S)-lyase](thiol form) = AMP + diphosphate + [citrate (pro-3S)-lyase](acetyl form)
show the reaction diagram
conversion of thiol form to acetyl form
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citrate lyase activation
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SYSTEMATIC NAME
IUBMB Comments
acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming)
Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
52660-22-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C2, DSM 614
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
associated with citrate lyase
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Manually annotated by BRENDA team
Leuconostoc citrovorum
associated with citrate lyase
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Manually annotated by BRENDA team
component of the citrate lyase cluster
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Manually annotated by BRENDA team
J1 strain, component of the citrate lyase cluster
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate + citrate (pro-3S)-lyase
?
show the reaction diagram
ATP + acetate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
ATP + acetate + citrate (pro-3S)-lyase (thiol form)
AMP + diphosphate + citrate(pro-3S)-lyase (acetyl form)
show the reaction diagram
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?
ATP + propionate + citrate (pro-3S)-lyase
AMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
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thiol form of (pro-3S)-lyase, propionate at 47% of the activity relative to acetate
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CTP + acetate + citrate (pro-3S)-lyase
CMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
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thiol form of (pro-3S)-lyase, CTP at 30% of the relative to ATP
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dATP + acetate + citrate (pro-3S)-lyase
dAMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
dTTP + acetate + citrate (pro-3S)-lyase
dTMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
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thiol form of (pro-3S)-lyase, dTTP at 5% of the activity relative to ATP
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GTP + acetate + citrate (pro-3S)-lyase
GMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
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thiol form of (pro-3S)-lyase, GTP at 43% of the activity of ATP
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ITP + acetate + citrate (pro-3S)-lyase
IMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
UTP + acetate + citrate (pro-3S)-lyase
UMP + diphosphate + citrate(pro-3S)-lyase
show the reaction diagram
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thiol form of (pro-3S)-lyase, UTP at 18% of the activity relative to ATP
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + acetate + citrate (pro-3S)-lyase
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PO43-
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activity is modulated by phosphorylation/dephosphorylation, active form of enzyme is phosphorylated
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.66 - 66
acetate
0.013
acetyl adenylate
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0.0008 - 0.4
ATP
0.000037 - 0.00386
citrate lyase
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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6: 50% of maximal activity, 8: 55% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37500
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gel filtration, density gradient centrifugation
41690
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1 * 41690, SDS-PAGE
56000
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1 * 56000, SDS-PAGE
58000
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gel filtration, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by nucleotides, most potent stabilizer is ADP
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cannot be co-purified with the citrate lyase subunits
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copurification of citrate lyase and citrate lyase ligase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the gene citC, which encodes the citrate lyase ligase, is expressed as a subunit of the citCDFG cluster in Escherichia coli
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