Information on EC 3.1.2.16 - citrate-lyase deacetylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.2.16
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RECOMMENDED NAME
GeneOntology No.
citrate-lyase deacetylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[citrate (pro-3S)-lyase](acetyl form) + 6 H2O = [citrate (pro-3S)-lyase](thiol form) + 6 acetate
show the reaction diagram
hydrolysis inactivates EC 4.1.3.6 citrate (pro-3S)-lyase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citrate lyase activation
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SYSTEMATIC NAME
IUBMB Comments
[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].
CAS REGISTRY NUMBER
COMMENTARY hide
58319-93-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Clostridium sphenoides
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Manually annotated by BRENDA team
no activity in Enterobacter aerogenes
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Manually annotated by BRENDA team
no activity in Escherichia coli
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Manually annotated by BRENDA team
no activity in Streptococcus diacetilactis
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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
[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
show the reaction diagram
additional information
?
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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
[citrate (pro-3S)-lyase](acetyl form) + H2O
[citrate (pro-3S)-lyase](thiol form) + acetate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
L-glutamate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
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induced by
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001
[citrate (pro-3S)-lyase](acetyl form)
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pH 7.2, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
L-glutamate
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pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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specific activity 1000 U/mg; specific activity 15.00 U/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7300
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2 * 7300, SDS-PAGE
14300
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 7300, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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half-life 20 min, effectively protected against heat inactivation by 100 mM L-glutamate, half-life 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses activity upon repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, purified enzyme stable for at least 6 months
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-20C, partly purified enzyme retains full activity for at least 1 year
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-20C, purified enzyme loses 20% of activity within 1 year during storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE