Information on EC 2.7.1.25 - adenylyl-sulfate kinase

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

EC NUMBER
COMMENTARY hide
2.7.1.25
-
RECOMMENDED NAME
GeneOntology No.
adenylyl-sulfate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Purine metabolism
-
-
sulfate activation for sulfonation
-
-
Sulfur metabolism
-
-
sulfate reduction
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:adenylyl-sulfate 3'-phosphotransferase
The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
CAS REGISTRY NUMBER
COMMENTARY hide
9012-38-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CW15, cell wall mutant
-
-
Manually annotated by BRENDA team
zebra fish
GenBank
Manually annotated by BRENDA team
strain AN1460
-
-
Manually annotated by BRENDA team
variety Nipponbare
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
Ueda, marine alga
-
-
Manually annotated by BRENDA team
hydrothermal vent tube worm
-
-
Manually annotated by BRENDA team
NodQ gene
-
-
Manually annotated by BRENDA team
puffer fish
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv. oryzae, Philippine race 6, raxQ gene
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the apk1 apk3 apk4 triple mutant combination is pollen lethal
metabolism
sulfate activation pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine 5'-O-(3-thiotriphosphate) + adenosine 5-phosphosulfate
ADP + 3'-thiophosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
535fold lower Vmax than with ATP
-
?
adenosine 5'-phosphosulfate + ATP
3'-phosphoadenosine 5'-phosphosulfate + ADP
show the reaction diagram
-
-
-
?
ATP + adenosine 5'-O-(2-fluorodiphosphate)
ADP + 3'-phosphoadenosine 5'-O-(2-fluorodiphosphate)
show the reaction diagram
-
15fold lower Vmax than with adenosine 5-phosphosulfate
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
-
-
-
-
?
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
dATP + adenosine 5-phosphosulfate
dADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
?
MgATP2- + adenosine 5'-phosphosulfate
MgADP- + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
?
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
show the reaction diagram
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
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively
EDTA
-
assay with 0.25 mM EDTA
NaCl
increased activity at high salt conditions, 100 mM
Zn2+
-
309% of activation with Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-Phosphoadenosine 5'-phosphosulfate
-
-
2,4,6-Trinitrobenzene sulfonate
2,6-dichlorophenol indophenol
3'-phosphoadenosine 5'-phosphosulfate
-
product inhibition
4-Aminophenylacetate
-
0.008 mM, 50% inhibition
adenosine 5'-phosphosulfate
adenosine-5'-phosphosulfate
adenylyl sulfate
adenylyl sulfate acts as a strong uncompetitive inhibitor of the APS kinase reaction
ADP
-
free form, reverse reaction, weak
ammonium sulfate
-
high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
Bromosuccinimide
Cd2+
-
in excess
Cu2+
-
2 mM, 90% inhibition
dehydroascorbate
diethyldicarbonate
-
in the presence or absence of ATP-sulfurylase
ferricyanide
-
0.05 mM, complete inhibition
iodoacetamide
-
strong inhibition, dithiothreitol partially protects
Mercuriphenylacetate
Mn2+
-
in excess, activating below
N-ethylmaleimide
-
0.02 mM, 50% inhibition
NaClO3
-
6.57 mM, 50% inhibition of brain PAPSS activity, 3.26 mM, 50% inhibition of liver PAPSS
oxidized glutathione
p-chloromercuribenzoate
-
0.005 mM, 50% inhibition
reduced glutathion
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
-
high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
ascorbate
-
activation
dithioerythritol
-
2 mM, 200% activation
dithiothreitol
glutathione
High ionic strength
maximal activity at a high concentration of buffer-salts either alone or plus dithiothreitol and thioredoxin 1 from Escherichia coli
-
L-cysteine
-
activation
Na2SO3
-
5 mM, 200% activation
thioredoxin
Thioredoxin f
-
from spinach, 0.002 mg, 3fold activation in the presence of saturating concentrations of thiols
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.37
3'-phosphoadenosine 5'-phosphosulfate
0.06
adenosine 5'-O-(3-thiotriphosphate)
-
pH 8.0
0.00014 - 0.042
adenosine 5'-phosphosulfate
0.00044 - 0.00072
adenosine-5'-phosphosulfate
0.002 - 0.0046
adenylyl sulfate
0.007 - 1.9
ATP
0.13
MgADP-
0.14 - 2.4
MgATP2-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
adenosine 5'-O-(3-thiotriphosphate)
Escherichia coli
-
pH 8.0
14.1 - 272
adenosine 5'-phosphosulfate
50
adenosine 5-phosphosulfate
Escherichia coli
-
pH 8.0, 30°C
2.17 - 5
adenosine-5'-phosphosulfate
0.17 - 0.364
adenylyl sulfate
1.7 - 4.4
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31000 - 567000
adenosine 5'-phosphosulfate
425
4917 - 6950
adenosine-5'-phosphosulfate
6169
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 0.048
adenosine 5'-phosphosulfate
0.00058
adenosine-5'-phosphosulfate
-
wild type enzyme, at pH 8.0 and 25°C
0.017 - 0.029
adenylyl sulfate
0.61
ATP
-
wild type enzyme, at pH 8.0 and 25°C
additional information
adenylyl sulfate
no inhibition of a deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N; no inhibition of mutant R37A; no inhibition of mutant R40A
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.7 - 17
sulfate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00016
-
recombinant enzyme
0.000298
-
wild type activity, specific activities given for all mutant enzymes
0.002 - 0.006
-
-
0.12
pH 8.0. 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
in MES-Tricine-HEPES buffer
6.8
-
in imidazole buffer
6.8 - 7
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
approx. 80% of maximal activity at pH 5.5, approx. half-maximal activity at pH 8.5
6 - 8
-
approx. 80% of maximal activity at pH 6.0, approx. 65% of maximal activity at pH 8.0, imidazole buffer
6 - 8.5
-
approx. 70% of maximal activity at pH 6.0, approx. 75% of maximal activity at pH 8.5, MES-Tricine-HEPES buffer
6.8 - 8
7.5 - 9
-
approx. half-maximal activity at pH 7.5, approx. 80% of maximal activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
PAPSS 1
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1
Manually annotated by BRENDA team
-
PAPSS 1
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoforms APK4, AK1, and APK2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aquifex aeolicus (strain VF5)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thiobacillus denitrificans (strain ATCC 25259)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14500
-
4 * 14500, SDS-PAGE
21000
-
2 * 21000, phosphorylated enzyme, SDS-PAGE; 4 * 21000, dephosphorylated enzyme, SDS-PAGE
22000
-
2 * 22000, SDS-PAGE
22321
-
x * 22321, deduced from DNA sequence of cysC coding region
23670
-
2 * 23670
26000
-
2 * 26000, SDS-PAGE
29500
-
in the presence of dithiothreitol, gel filtration
29786
-
x * 29786, deduced from nucleotide sequence
30000
-
2 * 30000, SDS-PAGE
31000
-
2 * 31000, dissociation
31977
x * 31977, deduced from nucleotide sequence
33000
-
2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C
40000 - 45000
-
gel filtration
44000
-
x * 44000, SDS-PAGE
49500 - 52000
-
gel filtration
50000
-
gel filtration
58000
-
gel filtration
59000 - 60000
-
gel filtration
60500
6 * 60500, calculated, crystall structure analysis
61000
-
gel filtration
68000
x * 68000, deduced from nucleotide sequence
80000
-
dephosphorylated enzyme, gel filtration
85000 - 90000
-
gel filtration
150000
gel filtration
162000
-
gel filtration
716000
-
2 * 716000, MALDI-TOF mass spectrometry, native mass by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homohexamer
6 * 60500, calculated, crystall structure analysis
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
enzyme is phosphorylated upon incubation with ATP, phosphorylation site is identified as Ser109, phosphorylated enzyme is kinetically competent
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop vapor diffusion at 25°C in 40% (v/v) ethanol, 1.0% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM MgATP
APSK isoform 1 in complex with beta,gamma-imidoadenosine-5'-triphosphate, Mg2+, and adenosine 5'-phosphosulfate, hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 200 mM MgCl2, and 15-17.5% (w/v) PEG 2000
-
in complex with adenosine 5'-phosphosulfate, hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.25, 200 mM MgCl2, and 15–17.5% (w/v) PEG 2000
-
; crystals are grown at room temperature using hanging drops containing equal volumes of protein and reservoir solution
crystal structures of the PAPSS1 APS-kinase domain in complex with APS and in complex with the products PAPS and ADP are solved, both structures of isolated domain, obtained in different crystal forms, reveal symmetrical dimers
-
hanging drop vapor diffusion method
-
in complex with ligands, hanging drop vapor diffusion method, using 0.2 M NH4NO3, 20% (w/v) PEG3350
crystals are grown in 1.7 M NaH2PO4, 300 mM K2HPO4 and 100 mM Na-succinate, pH 4.0 by hanging drop vapor diffusion at room temperature, crystal structure of E-ADP-APS ternary complex at 1.43 A, crystal structure of E-ADP binary complex at 2.0 A
-
in complex with AMP-PNP and adenosine-5'-phosphosulfate, hanging drop vapor diffusion method, using 0.1 M sodium cacodylate trihydrate, pH 6.5, 0.2 M magnesium acetate tetrahydrate, and 20% (w/v) PEG 8000
hanging-drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
below, reversible inactivation at 30°C, reactivation rate increases with increasing pH
641209
7
-
reversible inactivation at 42°C
641209
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 43
-
10 min incubation at 30°C and 35.5°C do not affect the enzyme's activity, however, treatments of 38.8°C and 41.6°C decrease its activity to 80% and 60% of control, respectively. Temperatures higher than 43°C almost completely deactivate the enzyme. After incubation at 25°C for 17, 26, 41 and 68 h, the enzyme activity is 91%, 109%, 101% and 114% of the control, respectively
35
-
inactivation above, reversible by cooling to 0-30°C
36
-
equilibrium between active and inactive enzyme form
37
-
no loss of activity after 2 h, recombinant enzyme
40
-
reversible inactivation above by subunit dissociation, kinetics, MgATP2- or MgADP- stimulate reactivation
43
-
reversible inactivation, t1/2: 1 min
60 - 100
-
1 min, 85% reversible inactivation
60
-
complete inactivation after 15 min
70
-
no significant loss of activity after 15 min
80
-
irreversible inactivation, t1/2: 47 min, pH 8, 0.023 mg protein/ml
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more stable in ampholyte polybuffer 74 than in Tris or imidazole buffers
-
rapid loss of activity in dilute solutions
recombinant enzyme is rapidly inactivated by dialysis, dilution or freezing even in the presence of glycerol
slow freezing can cause loss of activity
-
slow inactivation in dilute solutions, even at low temperatures
-
stable to ammonium sulfate precipitation
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
generation of atomic oxygen during the photodeoxygenation of 2,8-dihydroxymethyldibenzothiophene S-oxide is capable of oxidizing the enzyme at the regulatory thiol residues
-
722457
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable to prolonged storage
-
-70°C, recombinant APS kinase fusion protein, 1 year, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; protein solutions are applied on Blue-Sepharose columns and further purified by ion-exchange chromatography
alumina C-gamma gel, ammonium sulfate, hydroxyapatite, Cellex CM, unstable upon column chromatography
-
ammonium sulfate, Affi-gel blue, Matrix-gel green, Agarose A
-
ammonium sulfate, affinity chromatography, gel filtration, ion-exchange chromatography
-
ammonium sulfate, Blue Sepharose, Sephacryl S-200, PBE 94, Red Sepharose, phenyl-sepharose
-
ammonium sulfate, Giogel P2, Blue Sepharose, Sephacryl S-300, PBE 94
-
ammonium sulfate, phenyl-Sepharose, Q-Sepharose, Sephacryl S-300, hydroxylapatite, pentyl- agarose, aminohexyl agarose, ATP-agarose
-
ammonium sulfate, Sephacryl S-200, partially purified
-
ammonium sulfate, Sephacryl S-300, chromatofocusing, 2'5'-ADP-agarose
-
DEAE-Sepharose, Matrex gel blue A, phenyl Cellofine
-
immobilized metal ion affinity chromatography (Ni2+)
Ni-NTA column chromatography and Superdex-200 gel filtration
Ni-NTA column chromatography, Ni-NTA/benzamidine-Sepharose column chromatography, and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
Ni2+-column, recombinant enzyme
-
nickel affinity column chromatography and Superdex-200 gel filtration
-
PAP-agarose column chromatography
-
partial
protein solution is loaded on a Glutathione-Sepharose Fast Flow column and further purified by gel-filtration chromatography using Superdex 200
-
recombinant enzyme using His-tag
recombinant protein using His-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APS kinase domain (amino acids 25-227) of the PAPSS1 coding region are expressed as a GST-fusion protein in Escherichia coli
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
expressed in COS-1 and HEK293 cells
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-DE3
expression in Escherichia coli
expression in Escherichia coli as fusion protein with glutathione-S-transferase or maltose binding protein
-
expression in Escherichia coli cysD-mutant
-
expression of full-length PAPS synthase and 1-268 N-terminal fragment in COS-1 cells and Escherichia coli
expression of wild-type and S107A mutant enzyme in Escherichia coli
-
expresssion in Escherichia coli
-
in vitro transcription/translation
structural gene cysC
-
the APS-kinase domain (25-227 amino acid resiudes) of the PAPSS1 coding region are expressed as a GST-fusion protein in Escherichia coli BL-21
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C86A/C119A
-
the mutant is kinetically similar to the reduced wild type enzyme
D136A
-
the mutant displays drastically reduced affinity for adenosine 5'-phosphosulfate compared to the wild type enzyme
D136N
-
the mutant displays drastically reduced affinity for adenosine 5'-phosphosulfate compared to the wild type enzyme
R93A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme. The mutation modestly reduces kcat by 2fold and increases the Km for adenosine 5‘-phosphosulfate by 3fold
S182C
similar catalytic activity as wild-type
S182F
similar catalytic activity as wild-type
delta34N
deletion mutant lacking the first 34 N-terminal residues from APS kinase domain results in an enzyme with similar kinetic behaviour to the full-length domain
delta50N
deletion mutant lacking the first 50 N-terminal residues from APS kinase domain show no substrate inhibition by adenylyl sulfate and approximately half of the full-length's turnover number, crystal structure reveals an asymmetrical dimer
E531Q
identified as naturally occurring mutation, E531Q found in a single sample of an African-American’s subject, almost no effect of mutations when expressed in COS-1 or HEK293 cells
G427A/H428A
-
no APS kinase activity
R333C
identified as naturally occurring mutation, R333C found exclusively in Caucasian-American’s DNA, almost no effect of mutations when expressed in COS-1 or HEK293 cells
R37A
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
R40A
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
D87A
-
almost complete loss of activity
D87E
-
80% loss of activity
D87R
-
almost complete loss of activity
D89A
-
almost complete loss of activity
D89E
-
75% loss of activity
D89R
-
almost complete loss of activity
DN89ND
-
switch mutant, almost complete loss of activity
G79R
-
reduced APS kinase activity
G88A
-
less than 30% loss of kinase activity
G88D
-
almost complete loss of activity
G88R
-
almost complete loss of activity
K97A
-
no effect on activity
LD86DL
-
switch mutant, almost complete loss of activity
N90A
-
30% loss of kinase activity
N90Q
-
30% loss of kinase activity
R92A
-
complete loss of kinase activity
C541A
the mutant shows reduced activity compared to the wild type enzyme
C549A
the mutant shows increased activity compared to the wild type enzyme
C36A/C69A
-
the mutant is not inhibited by oxidized glutathione and shows activity reduced to 71%
S104A
-
similar properties as wild-type
S107A
-
similar properties as wild-type enzyme
S107C
-
similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket
S97A
-
similar properties as wild-type
S99A
-
similar properties as wild-type
T103A
-
similar properties as wild-type
Y109F
-
similar properties as wild-type, velocity curve is shifted to the far right
H23C
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
T61E
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
H23C
-
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
-
T61E
-
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
-
additional information
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