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
4.1.3.6
-
RECOMMENDED NAME
GeneOntology No.
citrate (pro-3S)-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
citrate = acetate + oxaloacetate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Citrate cycle (TCA cycle)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
citrase
-
-
-
-
citratase
-
-
-
-
citrate (pro-3S)-lyase
-
-
citrate aldolase
-
-
-
-
citrate lyase
-
-
-
-
citrate lyase
-
-
citrate oxaloacetate-lyase(pro-3S-COO- --> acetate)
-
-
-
-
citric aldolase
-
-
-
-
citridesmolase
-
-
-
-
citritase
-
-
-
-
lyase, citrate
-
-
-
-
additional information
-
can be dissociated into components, two of which are identical with ec 2.8.3.10 and ec 4.1.3. 34
CAS REGISTRY NUMBER
COMMENTARY
9012-83-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Aerobacter indologenes
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
biovar diacetylactis CRL264
-
-
Manually annotated by BRENDA team
subsp. diacetylactis
-
-
Manually annotated by BRENDA team
subsp. lactis biovar diacetilactis
-
-
Manually annotated by BRENDA team
Lactococcus lactis subsp. diacetylactis
subsp. diacetylactis
-
-
Manually annotated by BRENDA team
Leuconostoc citrovorum
-
-
-
Manually annotated by BRENDA team
subsp. cremonis
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
no activity in Chlorobium thiosulfatophilum
-
-
-
Manually annotated by BRENDA team
no activity in Rhodospirillum rubrum
-
-
-
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
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
acetate + oxaloacetate
citrate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Leuconostoc citrovorum
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
Leuconostoc citrovorum
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8R4N0
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8N0X4
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8R4N0
citrate fermentation pathway
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8N0X4
citrate fermentation pathway
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
-
work opposite to the citrate synthase reaction, involved in the control of the direction of carbon flow in the citric acid cycle
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
Lactococcus lactis subsp. diacetylactis
-
-
-
?
citrate
?
show the reaction diagram
-
constitutive enzyme
-
-
-
citrate
?
show the reaction diagram
-
regulated by concentration of intracellular L-Glu
-
-
-
citrate
?
show the reaction diagram
-
the enzyme is involved in citrate fermentation pathway
-
-
-
additional information
?
-
-
transcription of the operon encoding the citrate lyase complex is induced by acid stress
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
?
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
-
-
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8R4N0
citrate fermentation pathway
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
Q8N0X4
citrate fermentation pathway
-
r
citrate
acetate + oxaloacetate
show the reaction diagram
-
work opposite to the citrate synthase reaction, involved in the control of the direction of carbon flow in the citric acid cycle
-
-
?
citrate
?
show the reaction diagram
-
constitutive enzyme
-
-
-
citrate
?
show the reaction diagram
-
regulated by concentration of intracellular L-Glu
-
-
-
citrate
?
show the reaction diagram
-
the enzyme is involved in citrate fermentation pathway
-
-
-
additional information
?
-
-
transcription of the operon encoding the citrate lyase complex is induced by acid stress
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-(5''-phosphoribosyl)-3'-dephospho-coenzyme A
-
attached to the gamma subunit, i.e. apo-ACP, via phosphodiester linkage by CitX, resulting in the formation of holo-ACP
2'-(5''-phosphoribosyl)-3'-dephospho-coenzyme A
-
attached to the gamma subunit, i.e. apo-ACP, via a phosphodiester linkage to serine-14, CitG and CitX catalyze the initial formation of the precursor 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA and subsequent transfer to apo-citrate lyase with removal of diphosphate
2'-(5''-phosphoribosyl)-3'-dephospho-coenzyme A
-
CitG and CitX catalyze the initial formation of the precursor 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA and subsequent transfer to apo-citrate lyase with removal of diphosphate
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+
Co2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Cu2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Fe2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
Km: 3 mM; strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+. Mg2+ and Mn2+ are most effective
Mg2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+. Mg2+ is most effective
Mg2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+. Mg2+ and Mn2+ are most effective
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
dependent
Mg2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+, Mg2+ is most effective
Mn2+
-
Km: 0.08 mM
Mn2+
-
Km: 0.08 mM; Mg2+ and Mn2+ are most effective divalent metal ions; strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
cooperative, binding of Mn2+ involves a conformational change in the enzyme complex
Mn2+
-
strict requirement for a divalent metal ion, Mg2+, Mn2+ or Co2+
Mn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
Zn2+
-
strictly dependent on the presence of a divalent metal cation: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
divalent cation required: Mg2+, Zn2+, Mn2+, Co2+ or Cu2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
inhibits activation by divalent metal ions
hydroxylamine
-
reversed with acetic anhydride
additional information
-
rate of reaction inactivation of the S. diacetilactis enzyme is about 1/10 of that of the Klebsiella aerogenes enzyme
-
additional information
-
reaction inactivation
-
additional information
Lactococcus lactis subsp. lactis, Leuconostoc citrovorum
-
weak reaction inactivation
-
additional information
-
reaction inactivation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
L-Glu
-
activity is strictly dependent on presence of L-Glu
L-Glu
-
addition of L-Glu is not necessary for activity and stabilization of the enzyme
pantothenate
-
contains 3.5 mol pantothenate per mol of enzyme in the acyl-carrier-protein gamma-subunit
phosphopantetheine
-
contains an acetyl group at its active site, the group is in thioester linkage probably on phosphopantetheine
phosphopantetheine
-
the prosthetic group probably resembles 4'-phosphopantheteine
phosphopantothenate
-
contains 3 mol of phosphopantothenate per mol of enzyme
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
citrate
-
-
0.17
-
citrate
-
with 2 mM Mg2+
0.21
-
citrate
-
-
0.31
-
citrate
-
with 5 mM Mg2+
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.003
-
-
tryptone and yeast extract as growth substrates
0.009
-
-
H2, acetate and yeast extract as growth substrates
0.025
-
-
H2 and CO2 as growth substrates
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
8
-
in 100 mM tris-HCl buffer or 100 mM potassium phosphate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
9
-
pH 6.8-8.0: pH-optimum, pH 9.0: more than 80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
45
-
50% activity at 45C, 75% activity at 30C, 8.3% activity at 22C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
for DNA isolation
Manually annotated by BRENDA team
Q8R4N0
moderate expression
Manually annotated by BRENDA team
Q8R4N0
moderate expression
Manually annotated by BRENDA team
Q8R4N0
moderate expression
Manually annotated by BRENDA team
Q8R4N0
moderate expression
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia xenovorans (strain LB400)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
11760
-
-
apo-ACP-His, mass spectrometry
12500
-
-
apo-ACP-His, SDS-PAGE
12650
-
-
holo-ACP-His, mass spectrometry
15000
-
-
holo-ACP-His, SDS-PAGE
515000
-
-
gel filtration, sucrose density gradient centrifugation
520000
-
-
equilibrium sedimentation
530000
-
-
equilibrium sedimentation
536600
-
-
gel filtration, sedimentation equilibrium centrifugation
550000
-
-
meniscus depletion equilibrium sedimentation
560000
-
-
gel filtration
580000
-
-
disc gel electrophoresis
585000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oligomer
-
x * 14000 + x * 34000 + x * 55000, SDS-PAGE
oligomer
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
oligomer
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
oligomer
-
x * 11900 + x * 33800 + x * 55800, SDS-PAGE
oligomer
-
x * 30000 + x * 61000, SDS-PAGE
oligomer
-
x * 11000 + x * 32000 + x * 54500, gel filtration in presence of 6 M guanidinium chloride
oligomer
-
alpha6beta6gamma, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000,acyl-carrier-protein gamma-subunit, SDS-PAGE
oligomer
-
x + 10000, + x * 32000, + x * 54000, SDS-PAGE
oligomer
-
alpha6beta6gamma6, 6 * 10427, gamma, + 6 * 31352, beta, + 6 * 54668, alpha, calculation from nucleotide sequence
oligomer
-
x * 11800, + x * 34000 + x * 56600, SDS-PAGE
?
-
alpha, beta, gamma
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
acetyl-enzyme
side-chain modification
-
-
side-chain modification
-
acetyl-enzyme; citrate-lyase-deacetylase functions as an S-acetyl enzyme thioester hydrolase, and catalyzes the conversion of the S-acetyl form of citrate lyase into the inactive sulfhydryl form by hydrolysis of acetyl-thioester bonds of the prosthetic group. In the presence of citrate the deacetylase is stronly inhibited and the deacetylated citrate lyase is is converted to the active acetyl-S-form by the citrate-lyase ligase
side-chain modification
-
contains an acetyl group at its active site, the group is in thioester linkage probably on phosphopantetheine
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 ACCESSION NO.
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
half-life: 4 h
30
-
-
24 h, 7% loss of activity
60
-
-
15 min, 9% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
only stable in presence of 150 mM L-Glu or 7 mM L-Glu plus glycerol, sucrose or bovine serum albumin
-
repeated freezing and thawing inactivates
-
bovine serum albumin, sucrose and MgSO4 greatly enhance storage stability of lyophilized enzyme preparation
-
Mg2+ or Ca2+ reduces the rate of inactivation of dilute solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for 2 months
-
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
-
4C, stable for 4 days
-
4C, pH 7.2, 100 mM potassium phosphate buffer, 3 mM MgCl2, 1 mM dithiothreitol, stable for 3 days
-
0C or -20C, stable in presence of ammonium sulfate
-
0C or -20C, stable for at least 2-3 days
-
0C, in presence of saturated ammium sulfate and MgSO4, stable
-
-20C, stable for at least 6 months
-
4C, stable for at least 1 month
-
4C, crystals suspended in 3 M ammonium sulfate, stable for 8 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme complex is associated with acetylating enzyme activity
-
apo-ACP, i.e. gamma-subunit
-
acetate:HS-citrate lyase ligase is associated with citrate lyase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-subunit
Q8N0X4
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
-
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
-
beta-subunit
Q8R4N0
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
polymorphisms of the citrate lyase gene, may be involved in appetite regulation and antipsychotic induced metabolic syndrome with olanzapine-induced weight gain, are analysed
analysis
-
analytical method for detection of adulteration of citrus products by a flow-injection method based on the use of enzyme reactors
analysis
-
determination of citrate in urine with a new citrate lyase method
analysis
-
quantification of citrate lyase by enzyme-linked immunosorbent assay for determining the population of Lactococcus lactis subsp. lactis biovar diacetilactis