Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase

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

EC NUMBER
COMMENTARY hide
2.3.1.9
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
condensation
-
-
-
-
thiolytic cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
-
-
2-methylpropene degradation
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
acetoacetate degradation (to acetyl CoA)
-
-
acetyl-CoA fermentation to butanoate II
-
-
crotonate fermentation (to acetate and cyclohexane carboxylate)
-
-
ethylmalonyl-CoA pathway
-
-
fermentation to 2-methylbutanoate
-
-
glutaryl-CoA degradation
-
-
isoprene biosynthesis II (engineered)
-
-
isopropanol biosynthesis (engineered)
-
-
ketogenesis
-
-
ketolysis
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
L-isoleucine degradation I
-
-
L-lysine fermentation to acetate and butanoate
-
-
levulinate degradation
-
-
methyl tert-butyl ether degradation
-
-
mevalonate pathway I
-
-
mevalonate pathway II (archaea)
-
-
mevalonate pathway III (archaea)
-
-
polyhydroxybutanoate biosynthesis
-
-
pyruvate fermentation to acetone
-
-
pyruvate fermentation to butanoate
-
-
pyruvate fermentation to butanol I
-
-
pyruvate fermentation to butanol II (engineered)
-
-
pyruvate fermentation to hexanol (engineered)
-
-
butanoate fermentation
-
-
CO2 fixation in Crenarchaeota
-
-
mevalonate metabolism
-
-
tryptophan metabolism
-
-
Fatty acid degradation
-
-
Synthesis and degradation of ketone bodies
-
-
Valine, leucine and isoleucine degradation
-
-
Lysine degradation
-
-
Benzoate degradation
-
-
Tryptophan metabolism
-
-
Pyruvate metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Propanoate metabolism
-
-
Butanoate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Terpenoid backbone biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-46-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mmgA
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
L. G. Don, herbarium number LEF 920116
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
haloarchaeon
-
-
Manually annotated by BRENDA team
haloarchaeon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
; adzuki bean borer moth, female moths, gene Osat1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
show the reaction diagram
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
acetyl-CoA + acetyldithio-CoA
CoA + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
show the reaction diagram
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-S-(11-methoxymethyl)pantetheine
acetyl-CoA + acetyl-S-(11-methoxymethyl)pantetheine
show the reaction diagram
-
-
-
-
?
CoA + acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
acetyl-CoA + acetyl-S-(11-t-butyldimethylsilyl)pantetheine
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(D-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(D-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(L-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(L-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-homopantetheine 12-pivalate
acetyl-CoA + acetyl-S-homopantetheine 12-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-pantetheine
acetyl-CoA + acetyl-S-pantetheine
show the reaction diagram
-
-
-
?
additional information
?
-
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
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
B7XEI5
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
show the reaction diagram
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme contains selenomethionine
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above 10 mM
Cl-
-
the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops
K+
-
the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops
Mn2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above
additional information
not stimulated by Ni2+, Ca2+ and Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11-Chloro-10-oxoundecanoic acid
-
acetyl-CoA or CoA protect
11-chloro-10-oxoundecanoyl-CoA
-
acetyl-CoA or CoA protect
-
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 1.9 min
2-Butynoyl-CoA
-
0.1 mM, 74% inactivation after 10 min
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
3-butynoyl-CoA
-
0.01 mM, 95% inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-hydroxybutyryl-CoA
-
-
3-Pentenoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 0.26 min
3-Pentynoyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentynoylpantetheine
-
1 mM, complete inactivation after 10 min
4-Bromocrotonyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
4-bromocrotonylpantetheine
-
1 mM, complete inactivation after 10 min
5,5'-dithiobis(2-nitrobenzoate)
-
0.4 mM, 87% inhibition
5-chloro-4-oxopentanoyl-CoA
-
acetyl-CoA or CoA protect
7-Chloro-6-oxoheptanoic acid
-
acetyl-CoA or CoA protect
7-chloro-6-oxoheptanoyl-CoA
-
acetyl-CoA or CoA protect
9-Chloro-8-oxononanoic acid
-
acetyl-CoA or CoA protect
9-chloro-8-oxononanoyl-CoA
-
acetyl-CoA or CoA protect
acetoacetyl-CoA
acetyl-CoA
-
-
Acryl-S-pantetheine 11-pivalate
-
-
ATP
-
10 mM, 41% inhibition
bromoacetyl oxoester
-
acetyl-pantetheine 11-pivalate analog
-
Bromoacetyl thioester
-
acetyl-pantetheine 11-pivalate analog
Bromoacetylamide
-
acetyl-pantetheine 11-pivalate analog
butyryl-CoA
-
1 mM, 42% inhibition
Ca2+
-
10 and 25 mM, 25 and 50% inhibition of thiolysis
citraconic anhydride
-
-
dec-3-ynoic acid
-
irreversible inhibition
Dithionitrobenzoate
-
low but significant inhibition
iodoacetamide
N-ethylmaleimide
p-chloromercuribenzoate
Sodium borohydride
sulfhydryl reagents
-
-
thiolactomycin
-
0.36 mM, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
-
maximal activity at 4.5 M
lovostatin
-
1.9fold activity increase in rats treated with lovostatin
NaCl
-
maximal activity at 4.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.025
acetoacatyl-CoA
-
0.21
acetoacetyl-10-bis-demethylpantetheine 11-pivalate
-
-
0.0038 - 0.18
acetoacetyl-CoA
0.12
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
0.074
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
cosubstrate CoA
0.073
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
0.25
acetoacetyl-S-homopantetheine 12-pivalate
-
-
0.46
acetoacetyl-S-pantetheine
-
-
0.0062 - 1.06
acetyl-CoA
0.0048 - 0.154
CoA
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
3-ketobutyryldithio-CoA
-
-
266
acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
-
-
-
0.0767 - 5000000
acetoacetyl-CoA
353
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
434
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
-
469
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
256
acetoacetyl-S-(L-pantetheine) 11-pivalate
-
-
177
acetoacetyl-S-homopantetheine 12-pivalate
-
-
14 - 174
acetoacetyl-S-pantetheine
2.1
acetyl-CoA
-
-
29.5
CoA
-
presence of Mg2+
900
thiolytic cleavage
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5600 - 31650
acetoacetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
11-Chloro-10-oxoundecanoic acid
-
-
0.0025
11-chloro-10-oxoundecanoyl-CoA
-
-
-
1.54
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
-
1.25
3-Pentenoyl-S-pantetheine 11-pivalate
-
-
0.025
3-Pentynoyl-CoA
-
-
0.013
4-Bromocrotonyl-CoA
-
-
0.015
5-chloro-4-oxopentanoyl-CoA
-
-
11.4
7-Chloro-6-oxoheptanoic acid
-
-
0.002
7-chloro-6-oxoheptanoyl-CoA
-
-
0.49
9-Chloro-8-oxononanoic acid
-
-
0.0014
9-chloro-8-oxononanoyl-CoA
-
-
0.0014 - 0.0016
acetoacetyl-CoA
0.006 - 0.12
CoA
10
dec-3-ynoic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
Rattus norvegicus
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
-
0.16
-
acetoacetyl-CoA synthesis
0.9
crude enzyme, at pH 8.9 and 25°C
13.2
purified native enzyme
15.78
purified recombinant enzyme
56
after 62.22fold purification, at pH 8.9 and 25°C
58.2
-
-
100 - 130
-
peroxisomal thiolase, thiolysis
412
-
thiolysis of acetoacetyl-CoA
506
-
thiolase II
additional information
-
assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay at
7
-
condensation
8.1 - 8.4
-
isoenzyme A and B, acetoacetyl-CoA synthesis
8.4
-
cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
9.5
-
thiolysis
10.5
-
synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
69% of maximal activity at pH 9.0
6 - 9
-
approx. 80% of maximal activity at pH 6.0, approx. 40% at pH 9.0
6.5 - 9.2
-
approx. 50% of maximal activity at pH 6.5 and pH 9.2, thiolysis
7 - 9
significant decrease in activiy below pH 7.0 or above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
-
mitochondrial acetoacetyl CoA thiolase is decreased by 80% in ulcerative colitis compared with control. Mitochondrial thiolase activity in ulcerative colitis does not correlate with clinical, endoscopic or histological indices of disease severity. Mitochondrial thiolase activity is reduced in the normal right colon mucosa of patients with left-sided ulcerative colitis
Manually annotated by BRENDA team
; low ACT1 expression
Manually annotated by BRENDA team
highest expression in roots and petals
Manually annotated by BRENDA team
isoform AACT! is primarily expressed in the vascular system
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain EA 2018)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
x * 30000, SDS-PAGE
39000
-
4 * 39000, SDS-PAGE
40495
-
4 * 40495, electrospray ionization mass spectroscopy
40598
4 * 40598, deduced from nucleotide sequence
41200
x * 41200, calculated, x * 40000, SDS-PAGE
41320
x * 41320, calculated from amino acid sequence
42444
x * 42444, calculated from sequence
43445
x * 43445, calculated, x * 43000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
47000
x * 47000, recombinant enzyme, SDS-PAGE
53000
x * 53000, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
63000
-
x * 63000, SDS-PAGE
84000
-
about, recombinant His-tagged enzyme, gel filtration
86496
-
x * 86496, deduced from nucleotide sequence
88712
-
x * 88712, MALDI-mass spectrometry
147600
-
isoenzyme B, sedimentation analysis
150000
-
isoenzyme A, gel filtration
151000
-
gel filtration, isoenzyme A and B
152000
154600
-
isoenzyme A, sedimentation analysis
155000
156000
-
sucrose density gradient sedimentation
160000
-
peroxisomal thiolase, gel filtration
164000
-
gel filtration
166000
-
gel filtration
169000
-
sedimentation equilibrium
170000
-
gel filtration
180000
185000
-
native thiolase, gel filtration
187000
-
recombinant thiolase, gel filtration
188000
-
gel filtration
190000
-
gel filtration
193000
-
native PAGE
240000
-
peroxisomal thiolase I, gel filtration
250000
-
cytosolic thiolase I, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
homotetramer
-
x-ray crystallography
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM phosphate-citrate pH 4.2, 10% (w/v) polyethylene glycol 3350, 200 mM sodium chloride
purified recombinant enzyme in apoform and with bound CoA, hanging drop vapor diffusion method, mixing 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.001 ml of reservoir solution containing 1.0 M ammonium sulfate, 0.1 M HEPES, pH 7.25, and equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase Mttt0182, PDB ID1ULQ, as a search model, structure modeling
purified recombinant enzyme in apoform or with bound CoA, hanging drop vapor diffusion method, mixing 0.0012 ml of 25 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.0012 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20-22°C, 7 days, X-ray diffraction structure determination and analysis at 1.4-1.5 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase MtFadA5, PDB ID 4UBU as a search model, structure modeling
-
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 140 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20°C, 7 days, X-ray diffraction structure determination and analysis at 1.4 A resolution
-
hanging drop vapor diffusion method at 4°C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
-
only successful in the presence of CoA
microbatch method, using either 20% (w/v) PEG 3350, 0.15 M calcium chloride dehydrate, or 45% (w/v) PEG 200, 0.1 M MES monohydrate pH 6.0, 0.07 M calcium chloride dehydrate or 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, 30% (w/v) PEG 8000, 5% (v/v) n-octyl-beta-D-glucoside
-
hangig-drop vapor diffusion at 21°C, crystal structure at 2.0 A resolution
-
wild-type thiolase and acetylated thiolase complexed with CoA, C89A mutant thiolase complexed with acetyl-CoA and acetoacetyl-CoA, Q64A mutant thiolase
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
1 h, complete loss of activity
37
-
wild-type T2 protein is stable even after chasing for 48 h at 37°C. The amount of E252del mutant protein at 48 h incubation with cycloheximide is estimated to be 50% of that observed at 0 h. E252del mutant T2 is unstable compared to the wild-type protein at 37°C
63
-
5 min, stable
70
-
10 h, 4 M KCl, 20% loss of activity
85
-
10 h, 4 M KCl, 35% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
glycerol stabilizes
-
labile enzyme, partially stabilized by 1-2 mM dithiothreitol and 20% ethylene glycol
-
more than 10% sucrose, 2-mercaptoethanol or dithiothreitol are necessary to maintain activity
-
unstable in dilute solution, less than 0.5 mg/ml protein
-
urea: 2.5 M, 17 h, 50% loss of activity, 5 M, 45 min, 50% loss of activity, 7 M, 1 min, 50% loss of activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to borohydride reduction
-
487690
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, less than 0.2 mg/ml protein, 50 mM Tris, pH 7.2, 0.5 mM dithiothreitol, 8 d, 60-70% loss of activity
-
-20°C, 20 mM Tris-HCl, pH 7.8, 0.5 mM 1 mM, EDTA, 15 d, loss of more than 50% activity