Information on EC 6.2.1.13 - acetate-CoA ligase (ADP-forming)

for references in articles please use BRENDA:EC6.2.1.13
Word Map on EC 6.2.1.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

EC NUMBER
COMMENTARY hide
6.2.1.13
-
RECOMMENDED NAME
GeneOntology No.
acetate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate and ATP formation from acetyl-CoA II
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
pyruvate fermentation to acetate III
-
-
acetyl CoA biosynthesis
-
-
Glycolysis / Gluconeogenesis
-
-
Pyruvate metabolism
-
-
Propanoate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
acetate:CoA ligase (ADP-forming)
Also acts on propanoate and, very slowly, on butanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
62009-85-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Giardia intestinalis WB / CC 30957
clone 6
SwissProt
Manually annotated by BRENDA team
strain DSM 5350
-
-
Manually annotated by BRENDA team
strain DSM 3757
-
-
Manually annotated by BRENDA team
strain DSM 1137
-
-
Manually annotated by BRENDA team
enzyme form ACS1; enzyme form ACS2
-
-
Manually annotated by BRENDA team
strain DSM 4184
-
-
Manually annotated by BRENDA team
gene acs
-
-
Manually annotated by BRENDA team
-
Q5JIA8 and Q5JIA9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme is a member of the NDP-forming acyl-CoA synthetase enzyme superfamily
malfunction
-
amoebae lacking enzyme activity are unable to reestablish the acetyl-CoA/CoA ratio after an oxidative stress challenge; gradual ACS gene silencing (49-93%) significantly decreases the acetate flux without affecting the levels of glycolytic metabolites and ATP in trophozoites. Amoebae lacking ACS activity are unable to reestablish the acetyl-CoA/CoA ratio after an oxidative stress challenge
metabolism
-
the enzyme is related to the phosphate-dependent fermentative glycolysis in Entamoeba histolytica. The end-products of carbohydrate catabolism in the parasite are ethanol and acetate, produced by the bifunctional aldehyde-alcohol dehydrogenase (ADHE) and ACS, respectively, overview; the main role of the enzyme in the parasite energy metabolism is to recycle CoA for glycolysis to proceed under aerobic conditions
physiological function
additional information
-
residue His252 is essential for enzymatic activity, substrate binding structure and mechanism, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
show the reaction diagram
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
show the reaction diagram
-
r, isoenzyme ACS II is active, ACS I not
-
-
-
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
show the reaction diagram
ADP + phosphate + isovaleryl-CoA
ATP + isovalerate + CoA
show the reaction diagram
less than 1% activity compared to acetyl-CoA
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
ADP + phosphate + propanoyl-CoA
ATP + propanoate + CoA
show the reaction diagram
45% of the activity relative to acetyl-CoA
-
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
show the reaction diagram
ATP + 3-methylthiopropionate + CoA
ADP + phosphate 3-methylthiopropionyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
ATP + heptanoate + CoA
ADP + phosphate + heptanoyl-CoA
show the reaction diagram
less than 4% activity compared to acetate
-
-
r
ATP + hexanoate + CoA
ADP + phosphate + hexanoyl-CoA
show the reaction diagram
less than 4% activity compared to acetate
-
-
r
ATP + imidazole-4-acetate + CoA
ADP + phosphate + imidazol-4-ylacetyl-CoA
show the reaction diagram
-
17% activity compared to acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
-
34% of the activity relative to acetate
-
-
-
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
show the reaction diagram
ATP + octanoate + CoA
ADP + phosphate + octanoyl-CoA
show the reaction diagram
less than 4% activity compared to acetate
-
-
r
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
show the reaction diagram
-
36% of the activity relative to acetate
-
-
-
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
less than 4% activity compared to acetate
-
-
r
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
show the reaction diagram
ATP + valerate + CoA
ADP + phosphate + valeryl-CoA
show the reaction diagram
less than 4% activity compared to acetate
-
-
r
CDP + phosphate + acetyl-CoA
CTP + acetate + CoA
show the reaction diagram
7% activity compared to ADP
-
-
r
CTP + acetate + CoA
CDP + phosphate + acetyl-CoA
show the reaction diagram
4.1% activity compared to ATP
-
-
r
dADP + phosphate + acetyl-CoA
dATP + acetate + CoA
show the reaction diagram
-
40% of the activity relative to ADP
-
-
-
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
show the reaction diagram
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
show the reaction diagram
ITP + acetate + CoA
IDP + phosphate + acetyl-CoA
show the reaction diagram
15% activity compared to ATP
-
-
r
UDP + phosphate + acetyl-CoA
UTP + acetate + CoA
show the reaction diagram
2.8% activity compared to ADP
-
-
r
UTP + acetate + CoA
UDP + phosphate + acetyl-CoA
show the reaction diagram
1.6% activity compared to ATP
-
-
r
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
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
oxidation to NAD+ by assay system lactate dehydrogenase and pyruvate kinase
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
inhibits the acetate-forming direction of the reaction
Ca2+
-
about 3% residual activity at 20 mM
Cu2+
-
about 15% residual activity at 20 mM
D-glucose 6-phosphate
-
-
diphosphate
-
inhibits the acetate-forming direction of the reaction (64% residual activity at 10 mM)
glyoxylate
-
32% residual activity at 10 mM
Isobutyrate
-
10 mM, complete inhibition
NaCl
-
2-3 M, 40% loss of activity
NAD+
-
47% residual activity at 10 mM
Ni2+
-
about 3% residual activity at 20 mM
Zn2+
-
about 5% residual activity at 20 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 14
acetate
0.0039 - 0.45
acetyl-CoA
0.015 - 1.9
ADP
0.0556 - 12
ATP
0.0056 - 1.6
CoA
1.09
dADP
-
-
0.132 - 1.9
GDP
0.43 - 10
GTP
0.132 - 0.457
Isobutyrate
0.012 - 0.04
isobutyryl-CoA
0.329
phenylacetate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
0.004 - 0.11
phenylacetyl-CoA
0.1 - 3.25
phosphate
5.2 - 29
propionate
0.032
propionyl-CoA
-
at pH 7.3 and 37C
0.322
thioglycolate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 240
acetate
0.12 - 157
acetyl-CoA
0.27 - 203
ADP
0.25 - 320
ATP
0.25 - 328
CoA
21 - 411
GDP
27 - 180
GTP
66
indoleacetate
-
isoenzyme ACS II
22 - 55
Isobutyrate
8 - 121
isobutyryl-CoA
40.6 - 89
phenylacetate
138
phenylacetyl-CoA
-
isoenzyme ACS II
0.22 - 182
phosphate
190
propionate
-
at pH 7.3 and 37C
21
propionyl-CoA
-
at pH 7.3 and 37C
26.1
thioglycolate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 58
acetate
0.06 - 2600
acetyl-CoA
0.2 - 89
ADP
0.07 - 965
ATP
0.57 - 9490
CoA
90
GDP
-
with acetyl-CoA as cosubstrate, at pH 7.3 and 37C
18
GTP
-
with acetate as cosubstrate, at pH 7.3 and 37C
385
Isobutyrate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
123
phenylacetate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
0.97 - 95
phosphate
6.3
propionate
-
at pH 7.3 and 37C
650
propionyl-CoA
-
at pH 7.3 and 37C
81
thioglycolate
Q5JIA8 and Q5JIA9
at pH 6.5 and 55C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.81
ATP
Entamoeba histolytica
-
at pH 7.3 and 37C
10
D-glucose 6-phosphate
Entamoeba histolytica
-
at pH 7.3 and 37C
0.83
diphosphate
Entamoeba histolytica
-
at pH 7.3 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
-
pH 9.0, at 37C, oxic conditions, during exponential growth phase on glucose
0.3
-
50C, pH not specified in the publication, enzyme from lactate-grown cells
0.45
-
pH 9.0, at 37C, oxic conditions, purified enzyme
30
-
isoenzyme ACS II
64.6
-
isoenzyme ACS I
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
forward reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
pH 5.5: about 40% of maximal activity, pH 7.5: about 20% of maximal activity
6 - 7
-
at pH 6.0-7.0, the recombinant enzyme shows 1560% of the maximum activity
6 - 11
-
6: about 60% of maximal activity, 11: about 40% of maximal activity, isoenzyme ACS I
6 - 8
-
about 50% of maximal activity at pH 6 and 8
6.5 - 8.5
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity
7 - 11
-
7: about 60% of maximal activity, 11: about 65% of maximal activity, isoenzyme ACS II
7.3 - 7.8
-
the pH optimum is at pH 7.5, with remaining activities of about 40% at pH 7.3 and 59% at pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
isoenzyme ACS1
60
-
assay at
80
E7FI45 and E7FHP1
assay at, catalytic arsenolysis of acetyl-CoA
87
Q9Y8L0, Q9Y8L1
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
20C: about 75% of maximal activity, 40C: about 45% of maximal activity, isoenzyme ACS1
25 - 55
-
25C: about 45% of maximal activity, 55C: about 40% of maximal activity, isoenzyme ACS2
25
-
isoenzymes ACS I and ACS II are inactive at
30 - 50
-
30C: about 50% of maximal activity, 50C: about 80% of maximal activity
37
-
the enzyme exhibits 70% activity at 37C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
estimation from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
25878
E7FI45 and E7FHP1
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
27000
E7FI45 and E7FHP1
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
45000
-
2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
49965
E7FI45 and E7FHP1
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
70000
-
x * 70000, isoenzyme ACS1, SDS-PAGE
75000
-
4 * 75000, native enzyme, SDS-PAGE
78000
estimation from sequence of cDNA
87000
-
2 * 87000, SDS-PAGE
140000
-
gel filtration
140000 - 150000
145000
150000
150000 - 165000
-
native PAGE
166000
-
gel filtration
300000
-
native enzyme, gel filtration
317000
-
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 70000, isoenzyme ACS1, SDS-PAGE; x * 77000, isoenzyme ACS2, SDS-PAGE
dimer
-
2 * 87000, SDS-PAGE
heterotetramer
homodimer
homotetramer
monomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
E7FI45 and E7FHP1
His257alpha and His71beta are sites of transient phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, sitting-drop vapour-diffusion method, crystals belong to monoclinic space group C2, with unit-cell parameters a = 131.3, b = 186.1, c = 121.5, beta = 122.6, and diffract at 2.0 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
-
half-life: 105 min
110
-
half-life is 30 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires high salt concentrations for long-term stability
-
salts stabilize against heat inactivation. In presence of 1 M KCl the enzyme does not lose activity after 2 h incubation
-
sensitivity towards heat inactivation is increased with storage at -20C
-
stability for more than 48 requires high salt concentrations, i.e., 1-2 M of KCl or NaCl
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to oxygen for 24 h
-
626
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1-2 mg/ml enzyme, in 20 mM Tris/HCl, pH 8.0, 2 mM MgCl2, 150 mM NaCl, stable for several weeks
-
-20C, 50% (v/v) glycerol, 4 weeks, no loss of activity
-
on ice stable for 2 d
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 10fold, 15 min at 80C and subsequent anion-exchange chromatography
Q9Y8L0, Q9Y8L1
Co2+ affinity column chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
-
gel filtration on a Superdex TM200 column
HisTrap HP nickel affinity column chromatography, and Superdex 200 gel filtration
-
ion-exchange chromatography
isoenzymes ACS I and ACS II
-
Ni-NTA affinity chromatography, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
nickel affinity column chromatography
-
partial, isoenzyme ACS1; partial, isoenzyme ACS2
-
recombinant wild-type and mutant enzyme subunits from Escherichia coli strain BL21(DE3) by heat precipitation at 90C for 30 min, followed by reconstitution of holoenzyme through hydrophobic interaction chromatography ultrafiltration, and gel filtration, the chromatographic steps are then repeated; wild-type end mutant enzymes
E7FI45 and E7FHP1
Resource Q column chromatography and Superdex 200 gel filtration
Q5JIA8 and Q5JIA9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acdIa and acdIb genes encoding alpha- and beta-subunit of ACD, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
E7FI45 and E7FHP1
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
Q5JIA8 and Q5JIA9
expressed in Escherichia coli Rosetta2(DE3) pLysS cells
-
expressed in Escherichia coli Rosetta2(DE3)pLysS cells
-
expression in Escherichia coli
overexpression in Escherichia coli
Q9Y8L0, Q9Y8L1
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3), quantitative RT-PCR enzyme expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced 10fold during growth on D-glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D674A
-
site-directed mutagenesis, the mutation does not eliminate the ability of ACD to be phosphorylated from either direction, although phosphorylation by ATP is reduced; the variant retains about 1% activity compared to wild type enzyme
D674E
-
the variant retains about 45% activity compared to wild type enzyme
D674N
-
the variant retains about 1% activity compared to wild type enzyme
E213A
-
site-directed mutagenesis, the mutant variant is not phosphorylated by acetyl-CoA and phosphate; the variant retains about 1% activity compared to wild type enzyme
E213D
-
the variant retains about 1% activity compared to wild type enzyme
E213Q
-
the variant retains about 1% activity compared to wild type enzyme
E218A
-
site-directed mutagenesis, the mutant variant is not phosphorylated by acetyl-CoA and phosphate
H252A
-
site-directed mutagenesis, alteration of His252 in EhACD effectively eliminate overall enzymatic activity as well as phosphorylation in either direction of the reaction; the variant has no detectable activity in either direction of the reaction
H533D
-
the variant retains about 3% activity compared to wild type enzyme
H533E
-
the variant retains about 1% activity compared to wild type enzyme
H533K
-
the variant retains about 10% activity compared to wild type enzyme
H533N
-
the variant retains about 5% activity compared to wild type enzyme
H533Q
-
the variant retains about 5% activity compared to wild type enzyme
H533R
-
the variant retains about 10% activity compared to wild type enzyme; the variant retains less than 25% activity compared to wild type enzyme
D212betaE
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced
E218alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced
E218alphaQ
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced
E218Dalpha
E7FI45 and E7FHP1
1-10% of wild-type activity
H257alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit
H257Dalpha
E7FI45 and E7FHP1
mutant shows no activity in either direction
H71betaA
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit
G266S
-
the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme
additional information
-
gradual ACS gene silencing (49-93%) significantly decreases the acetate flux without affecting the levels of glycolytic metabolites and ATP in trophozoites. Amoebae lacking ACS activity are unable to reestablish the acetyl-CoA/CoA ratio after an oxidative stress challenge
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed mixed and incubated on ice; equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed, mixed and incubated on ice
Q9Y8L0, Q9Y8L1
Show AA Sequence (203 entries)
Please use the Sequence Search for a specific query.