Information on EC 4.1.1.4 - Acetoacetate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
4.1.1.4
-
RECOMMENDED NAME
GeneOntology No.
Acetoacetate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetoacetate + H+ = acetone + CO2
show the reaction diagram
-
-
-
-
acetoacetate + H+ = acetone + CO2
show the reaction diagram
the enzyme catalyzes the reaction with net racemization
-
acetoacetate + H+ = acetone + CO2
show the reaction diagram
stereochemistry
-
acetoacetate + H+ = acetone + CO2
show the reaction diagram
mechanism
-
acetoacetate + H+ = acetone + CO2
show the reaction diagram
mechanism; Schiff base intermediate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
acetone degradation I (to methylglyoxal)
-
acetone degradation III (to propane-1,2-diol)
-
isopropanol biosynthesis
-
ketogenesis
-
pyruvate fermentation to acetone
-
Synthesis and degradation of ketone bodies
-
Propanoate metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
acetoacetate carboxy-lyase (acetone-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AAD
-
-
-
-
acetoacetic acid decarboxylase
-
-
acetoacetic acid decarboxylase
Clostridium beijerinckii AA243, Clostridium beijerinckii NCIMB 8052
-
-
-
acetoacetic acid decarboxylase
-
-
acetoacetic acid decarboxylase
-
-
Acetoacetic decarboxylase
-
-
-
-
ADC
-
-
-
-
CP 28/CP 29
-
-
-
-
Decarboxylase, acetoacetate
-
-
-
-
Polymyxin MI
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-03-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 824
-
-
Manually annotated by BRENDA team
strain ATCC 824
UniProt
Manually annotated by BRENDA team
strain EA 2018
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes K115C, K115Q, K116C, K116N and K116R
-
-
Manually annotated by BRENDA team
NCIMB 8052; strain AA243, no activity in
-
-
Manually annotated by BRENDA team
strain NRRL B592, and strain NRRL B593
-
-
Manually annotated by BRENDA team
Clostridium beijerinckii AA243
strain AA243, no activity in
-
-
Manually annotated by BRENDA team
in addition to the intracellular enzyme, the extracellular produced polymyxin MI catalyzes the reaction; strain A-57
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa A-57
strain A-57
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
A6M020
enzyme AADC-catalyzed decarboxylation of acetoacetate is not the sole means for acetone generation
physiological function
-
enzyme AADC-catalyzed decarboxylation of acetoacetate is not the sole means for acetone generation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-2-Methyl-3-oxobutyrate
Butane-2-one + CO2
show the reaction diagram
-
-
-
-
-
(-)-2-Oxocyclohexanecarboxylate
Cyclohexanone + CO2
show the reaction diagram
-
-
-
-
-
2,4-pentanedione
?
show the reaction diagram
Q7NSA6
-
-
-
?
2-Oxo-3-phenylpropionic acid
Acetophenone + CO2
show the reaction diagram
-
i.e. phenylacetoacetate
-
-
-
3-oxopentanoate + H+
2-butanone + CO2
show the reaction diagram
-
-
-
?
3-oxopentanoate + H+
2-butanone + CO2
show the reaction diagram
-
-
products are obtained when heptanoate and not octanoate, pentanoate, decanoate or nonanoate are used as a carbon source in cultures, non-enzymatic decarboxylation is not discarded
?
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
Acetoacetate
Acetone + CO2
show the reaction diagram
-
-
-
-
?
Acetoacetate
Acetone + CO2
show the reaction diagram
Paenibacillus polymyxa A-57
-
-
-
-
Acetoacetate
?
show the reaction diagram
-
induction by linear acids from C1 to C4, whereas branched acids and linear acids from C5 to C7 are not inducers
-
-
-
Acetoacetate
?
show the reaction diagram
-
the enzyme is involved in the metabolic pathway of isopropanol
-
-
-
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
P23670
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
Q7NSA6
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
P23670
the AADC activity relies on measurement of CO2 produced as a result of AADC-catalyzed decarboxylation of acetoacetate
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020
the AADC activity relies on measurement of CO2 produced as a result of AADC-catalyzed decarboxylation of acetoacetate
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020, -
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020, -
the AADC activity relies on measurement of CO2 produced as a result of AADC-catalyzed decarboxylation of acetoacetate
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
Clostridium beijerinckii AA243
-
-
-
?
acetoacetate + proton
acetone + CO2
show the reaction diagram
-
-
-
?
levulinic acid + H+
2-butanone + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
catalyzes the exchange of deuterium or tritium into the alpha position of cyclohexanone or 2-butanone
-
-
-
additional information
?
-
-
acetoacetate decarboxylase from Clostridium acetobutylicum can act as a biocatalyst for decarboxylation of levulinic acid
-
-
-
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
Acetoacetate
?
show the reaction diagram
-
induction by linear acids from C1 to C4, whereas branched acids and linear acids from C5 to C7 are not inducers
-
-
-
Acetoacetate
?
show the reaction diagram
-
the enzyme is involved in the metabolic pathway of isopropanol
-
-
-
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
P23670
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
A6M020, -
-
-
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
Clostridium beijerinckii AA243
-
-
-
?
additional information
?
-
-
acetoacetate decarboxylase from Clostridium acetobutylicum can act as a biocatalyst for decarboxylation of levulinic acid
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenyl acetate
-
acetylation and complete inactivation of the enzyme
2-oxopropane sulfonate
-
-
Acetic anhydride
-
acetylation and complete inactivation of the enzyme
Acetonylphosphonate
-
competitive, rapidly dissociating
Acetopyruvate
-
the enzyme inhibitor compound is an enamine, obtained by the tautomerization of the Schiff base initially formed from inhibitor and enzyme
Acetylacetone
-
potent, reversible
Azure B
-
slight inhibition at 2-10 mM
-
beta-Diketones
-
-
-
Borohydride
-
acetylacetone or NO3- protects
Borohydride
-
borohydride plus acetoacetate or 2-oxopropane sulfonate irreversibly inhibits, without affecting the latent decarboxylase. Monovalent anions protect
HCN-
-
inhibitory synergism between cyanide and carbonyl compounds. The effectiveness in descending order: acetaldehyde, acetone, cyclohexanone, methyl ethyl ketone, 3-hexanone, diethyl ketone
levulinic acid
-
substrate inhibition is observed with levulinic acid concentration higher than 5 mM
methylene blue
-
complete inhibition at 2 mM
Monovalent anions
-
at pH 7.0 and above, monovalent anions are entirely noncompetitive inhibitors, as the pH is lowered the inhibition becomes increasingly uncompetitive
-
Monovalent anions
-
-
-
p-Chloromercuriphenyl sulfonate
-
-
p-Chloromercuriphenyl sulfonate
-
reversal by Cys
Sodium-2-oxo-propanesulfonate
-
competitive
Zn2+
-
inhibits at above 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
activates about 2fold at 5-10 mM
-
acetate
-
in pH-controlled cultures, the addition of 20 mM acetate promotes a more vigorous solventogenic fermentation
Butyrate
-
in pH-controlled cultures, the addition of 20 mM acetate promotes a more vigorous solventogenic fermentation
methyl viologen
-
activates 6.7fold at 10 mM
spo0A
-
in gel retardation assays, the C-terminal domains of Spo0A is able to bind fragments of acetoacetate decarboxylase promoter, Spo0A directly controls the shift between acidogenesis and solventogenesis, insertional inactivation of spo0A blocked the formation of solvents
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
3-oxo-3-phenylpropionic acid
-
-
0.94
-
acetoacetate
-
-
4.1
-
acetoacetate
-
at 25C, in 50 mM phosphate buffer, pH 5.95
5.2
-
acetoacetate
-
-
5.7
-
acetoacetate
-
at 25C, in 50 mM phosphate buffer, pH 5.95
8.2
-
acetoacetate
-
wild-type enzyme
8.4
-
acetoacetate
-
mutant enzyme K116C
10
-
acetoacetate
-
mutant enzyme K116N
14.7
-
acetoacetate
-
mutant enzyme K116R
400
-
acetoacetate
-
polymyxin MI
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
30
-
acetoacetate
-
mutant enzyme K116N
38
-
acetoacetate
-
mutant enzyme K116C
165
-
acetoacetate
-
at 25C, in 50 mM phosphate buffer, pH 5.95
302
-
acetoacetate
-
mutant enzyme K116R
349
-
acetoacetate
-
at 25C, in 50 mM phosphate buffer, pH 5.95
1560
-
acetoacetate
-
wild-type enzyme
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0007
-
2,4-Pentanedione
-
at 25C, in 50 mM phosphate buffer, pH 5.95
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
with levulinic acid
6
-
-
polymyxin MI
6
-
-
wild-type enzyme
6
-
-
with acetoacetate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
8
-
pH 3: about 50% of maximal activity, pH 8: about 40% of maximal activity
3.5
8
-
activity range, profile overview
5
8
-
pH 5: about 40% of maximal activity, pH 8: about 25% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
45
-
over 30% of maximal activity at 20C and 45C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Paenibacillus polymyxa A-57
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Paenibacillus polymyxa A-57
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
33000
-
-
native PAGE
280000
-
-
gel filtration
340000
-
-
meniscus depletion method
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
about 10 * 27000, SDS-PAGE
?
-
x * 29000, meniscus depletion method in presence of 6 M guanidium chloride or 4 M urea
?
-
x * 27519, calculation from nucleotide sequence
?
Paenibacillus polymyxa A-57
-
about 10 * 27000, SDS-PAGE
-
homodecamer
-
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AAD complexed with 2,4-pentanedione, hanging drop vapor diffusion method, using 18-20% (v/v) glycerol, 40 mM phosphate buffer, pH 5.95, 100 mM sarcosine and 14-15% (w/v) PEG 3350
-
AAD complexed with 2,4-pentanedione, hanging drop vapor diffusion method, using 18-20% (v/v) glycerol, 40 mM phosphate buffer, pH 5.95, 100 mM sarcosine and 14-15% (w/v) PEG 3350
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
or lower, rapid and irreversible denaturation
4
9
-
25C, stable
5.5
9
-
4C, 23 h, stable
10
-
-
or higher, rapid and irreversible denaturation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
pH 4-9, stable
60
-
-
30 min, stable up to
70
-
-
above, biphasic irreversible inactivation
80
-
-
30 min, complete inactivation
80
-
-
30 min: 50% loss of activity, without addition of acetylacetone, stable in presence of 1 mM acetylacetone
85
-
-
30 min: 86% loss of activity, without addition of acetylacetone, stable in presence of 10 mM acetylacetone
additional information
-
-
acetylacetone protects against thermal inactivation
additional information
-
-
acetylacetone protects against thermal inactivation; biphasic thermal inactivation. Acetylacetone protects more effectively in preventing the rapid phase than in preventing the slow phase of activity loss
additional information
-
-
some enzyme is expressed and an equal amount is latent and may be measured only after its exposure to heat
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
rather easily inactivated by urea, guanidinium chloride and SDS
-
the enzyme dissociates into subunit dimers at pH 8 in 4 M urea solution at low temperature. The subunit dimers can be reassociated to form native, active enzyme by diluting the urea solution with phosphate buffer at pH 6.0 in the presence of dithiothreitol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and S-200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and S-200 gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain JM109
P23670
expressed in Escherichia coli strains ATCC 11303 and TA11
-
expression in Escherichia coli
-
gene aadc, cloning in Escherichia coli strain DH5alpha, expression as GFP-tagged enzyme
P23670
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), best induction over 24 h at 20C with 1 mM IPTG
-
gene aadc encoded in the sol operon, cloning of gene fragments aadc358-1 and aadc358-2 in Escherichia coli strain DH5alpha, expression as GFP-tagged enzyme
A6M020
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E61Q
-
the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)
E76Q
-
the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits aslight downward shift of the pH optimum
E76Q
-
the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation
R29Q
-
the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4
E61Q
-
the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)
E76Q
-
the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits a slight downward shift of the pH optimum
E76Q
-
the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation
K115C
-
mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities
K115Q
-
mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities
additional information
-
the butanol ratio increases from 70% to 80.05%, with acetone production reduced to approximately 0.21 g/l in the adc-disrupted mutant 2018adc
R29Q
-
the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4
additional information
-
the butanol ratio increases from 70% to 80.05%, with acetone production reduced to approximately 0.21 g/l in the adc-disrupted mutant 2018adc
-
additional information
A6M020
generation of an aadc deletion mutant, the mutant produces a maximum acetone concentration comparable to that produced by wild-type. Non-enzymatic decarboxylation of acetoacetate in vitro, under conditions similar to in vivo acetone-butanol-ethanol fermentation, produces 1.3 to 5.2 g/L acetone between pH 4.0-6.5 and explains why various knock-out and knockdown strategies designed to disrupt aadc in solventogenic Clostridium species do not eliminate acetone production during acetone-butanol-ethanol fermentation
additional information
-
generation of an aadc deletion mutant, the mutant produces a maximum acetone concentration comparable to that produced by wild-type. Non-enzymatic decarboxylation of acetoacetate in vitro, under conditions similar to in vivo acetone-butanol-ethanol fermentation, produces 1.3 to 5.2 g/L acetone between pH 4.0-6.5 and explains why various knock-out and knockdown strategies designed to disrupt aadc in solventogenic Clostridium species do not eliminate acetone production during acetone-butanol-ethanol fermentation
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
acetoacetate decarboxylase from Clostridium acetobutylicum can act as a biocatalyst for decarboxylation of levulinic acid in an enzymatic system for synthesis of 2-butanone from levulinic acid
analysis
-
the enzyme is a valuable tool for clinical analysis of ketone bodies in human plasma
analysis
Paenibacillus polymyxa A-57
-
the enzyme is a valuable tool for clinical analysis of ketone bodies in human plasma
-