Information on EC 4.1.3.6 - citrate (pro-3S)-lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
4.1.3.6
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RECOMMENDED NAME
GeneOntology No.
citrate (pro-3S)-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
citrate = acetate + oxaloacetate
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citric acid cycle
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SYSTEMATIC NAME
IUBMB Comments
citrate oxaloacetate-lyase (forming acetate from the pro-S carboxymethyl group of citrate)
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.10 (citrate CoA-transferase) and EC 4.1.3.34 (citryl-CoA lyase). EC 3.1.2.16, citrate lyase deacetylase, deacetylates and inactivates the enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aerobacter indologenes
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
beta-subunit
UniProt
Manually annotated by BRENDA team
beta-subunit
UniProt
Manually annotated by BRENDA team
Lactococcus lactis subsp. diacetylactis
subsp. diacetylactis
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-
Manually annotated by BRENDA team
Leuconostoc citrovorum
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-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
no activity in Chlorobium thiosulfatophilum
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-
-
Manually annotated by BRENDA team
no activity in Rhodospirillum rubrum
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-
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Manually annotated by BRENDA team
strain DSM 4184, grown at 95C autotrophically, heterotrophically, and mixotrophically with acetate, H2, and small amounts of yeast extract and with thiosulfate as the terminal electron acceptor
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + oxaloacetate
citrate
show the reaction diagram
citrate
?
show the reaction diagram
citrate
acetate + oxaloacetate
show the reaction diagram
additional information
?
-
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transcription of the operon encoding the citrate lyase complex is induced by acid stress
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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
?
show the reaction diagram
citrate
acetate + oxaloacetate
show the reaction diagram
additional information
?
-
-
transcription of the operon encoding the citrate lyase complex is induced by acid stress
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-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-(5''-phosphoribosyl)-3'-dephospho-coenzyme A
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
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divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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inhibits activation by divalent metal ions
hydroxylamine
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reversed with acetic anhydride
oxaloacetate
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pantothenate
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contains 3.5 mol pantothenate per mol of enzyme in the acyl-carrier-protein gamma-subunit
phosphopantetheine
phosphopantothenate
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contains 3 mol of phosphopantothenate per mol of enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.31
citrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
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tryptone and yeast extract as growth substrates
0.009
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H2, acetate and yeast extract as growth substrates
0.025
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H2 and CO2 as growth substrates
0.07 - 0.09
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8
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in 100 mM tris-HCl buffer or 100 mM potassium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 9
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pH 6.8-8.0: pH-optimum, pH 9.0: more than 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 45
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50% activity at 45C, 75% activity at 30C, 8.3% activity at 22C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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for DNA isolation
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia xenovorans (strain LB400)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
515000
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gel filtration, sucrose density gradient centrifugation
520000
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equilibrium sedimentation
530000
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equilibrium sedimentation
536600
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gel filtration, sedimentation equilibrium centrifugation
550000
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meniscus depletion equilibrium sedimentation
560000
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gel filtration
580000
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disc gel electrophoresis
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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alpha, beta, gamma
oligomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
additional information
-
citrate lyase activity observed only when an acetylating compound is present in the assay mixture, acetylation possibly involved in the regulation of activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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15 min, 9% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin, sucrose and MgSO4 greatly enhance storage stability of lyophilized enzyme preparation
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Mg2+ or Ca2+ reduces the rate of inactivation of dilute solutions
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only stable in presence of 150 mM L-Glu or 7 mM L-Glu plus glycerol, sucrose or bovine serum albumin
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repeated freezing and thawing inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 2 months
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-20C, stable for at least 6 months
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0C or -20C, stable for at least 2-3 days
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0C or -20C, stable in presence of ammonium sulfate
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0C, 30% glycerol, 40% sucrose or 10 mg per ml bovine serum albumin, 7 mM L-Glu, only some loss of activity after 5 min
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0C, in presence of saturated ammium sulfate and MgSO4, stable
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4C, crystals suspended in 3 M ammonium sulfate, stable for 8 months
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4C, pH 7.2, 100 mM potassium phosphate buffer, 3 mM MgCl2, 1 mM dithiothreitol, stable for 3 days
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4C, stable for 4 days
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4C, stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetate:HS-citrate lyase ligase is associated with citrate lyase
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apo-ACP, i.e. gamma-subunit
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the enzyme complex is associated with acetylating enzyme activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-subunit
expression of the citCDEFG gene cluster in Escherichia coli. The gene product of citD is the gamma-subunit of citrate lyase. The gene product of citE is the beta-subunit of citrate lyase. The gene product of citF is the alpha-subunit of citrate lyase. The enzyme synthesized in Escherichia coli lacks its prosthetic group and is active only in the presence of acetyl-CoA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
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polymorphisms of the citrate lyase gene, may be involved in appetite regulation and antipsychotic induced metabolic syndrome with olanzapine-induced weight gain, are analysed
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