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Information on EC 2.7.1.25 - adenylyl-sulfate kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q43295
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2.7.1.25 adenylyl-sulfate kinaseIUBMB Comments
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).
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Word Map
- 2.7.1.25
- chrysogenum
-
sulfate-activating
- 3'-phosphate
-
sulphurylase
-
2.7.7.4
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brachymorphic
- cysd
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molybdolysis
-
spondyloepimetaphyseal
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atp-sulphurylase
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aps kinase, papss1, aps-kinase, paps synthetase, papss, paps synthase, adenosine-5'-phosphosulfate kinase, adenosine 5'-phosphosulfate kinase, mxan3487, adenylylsulfate kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenosine-5'-phosphosulfate synthetase
-
-
-
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5'-phosphoadenosine sulfate kinase
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-
-
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adenosine 5'-phosphosulfate kinase
adenosine phosphosulfate kinase
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-
-
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adenosine phosphosulfokinase
-
-
-
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adenosine-5'-phosphosulfate 3'-phosphotransferase
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-
-
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adenosine-5'-phosphosulfate-3'-phosphokinase
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-
-
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adenosine-5'phosphosulfate kinase
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-
-
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adenylylsulfate 3'-phosphotransferase
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-
-
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adenylylsulfate kinase
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-
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APS kinase
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-
-
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ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
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-
-
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kinase, adenylylsulfate (phosphorylating)
-
-
-
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adenosine 5'-phosphosulfate kinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
9012-38-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-phosphosulfate
uncompetitive inhibition above 0.001 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
activity declines rapidly in the absence of dithiothreitol
high ionic strength
maximal activity at a high concentration of buffer-salts either alone or plus dithiothreitol and thioredoxin 1 from Escherichia coli
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00043
adenosine 5'-phosphosulfate
oxidized wild type enzyme, at pH 7.5 and 25°C
0.00048
adenosine 5'-phosphosulfate
reduced wild type enzyme, at pH 7.5 and 25°C
0.00048
adenosine 5'-phosphosulfate
wild type enzyme, at pH 7.5 and 17°C
0.0007
adenosine 5'-phosphosulfate
mutant enzyme D136N, at pH 7.5 and 17°C
0.00087
adenosine 5'-phosphosulfate
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.00092
adenosine 5'-phosphosulfate
mutant enzyme D136A, at pH 7.5 and 17°C
0.0019
adenosine 5'-phosphosulfate
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.00043
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17°C
0.00048
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17°C
0.00172
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17°C
0.00263
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.1
adenosine 5'-phosphosulfate
oxidized wild type enzyme, at pH 7.5 and 25°C
29
adenosine 5'-phosphosulfate
mutant enzyme D136A, at pH 7.5 and 17°C
45
adenosine 5'-phosphosulfate
mutant enzyme D136N, at pH 7.5 and 17°C
203
adenosine 5'-phosphosulfate
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C
239
adenosine 5'-phosphosulfate
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C
272
adenosine 5'-phosphosulfate
reduced wild type enzyme, at pH 7.5 and 25°C
272
adenosine 5'-phosphosulfate
wild type enzyme, at pH 7.5 and 17°C
14.1
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17°C
82.3
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17°C
136
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17°C
272
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31000
adenosine 5'-phosphosulfate
mutant enzyme D136A, at pH 7.5 and 17°C
32800
adenosine 5'-phosphosulfate
oxidized wild type enzyme, at pH 7.5 and 25°C
64000
adenosine 5'-phosphosulfate
mutant enzyme D136N, at pH 7.5 and 17°C
125000
adenosine 5'-phosphosulfate
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C
233000
adenosine 5'-phosphosulfate
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C
567000
adenosine 5'-phosphosulfate
reduced wild type enzyme, at pH 7.5 and 25°C
567000
adenosine 5'-phosphosulfate
wild type enzyme, at pH 7.5 and 17°C
31300
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17°C
32700
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17°C
189000
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17°C
567000
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00251
adenosine 5'-phosphosulfate
oxidized wild type enzyme, at pH 7.5 and 25°C
0.0328
adenosine 5'-phosphosulfate
mutant enzyme D136N, at pH 7.5 and 17°C
0.0348
adenosine 5'-phosphosulfate
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.0375
adenosine 5'-phosphosulfate
reduced wild type enzyme, at pH 7.5 and 25°C
0.0375
adenosine 5'-phosphosulfate
wild type enzyme, at pH 7.5 and 17°C
0.0416
adenosine 5'-phosphosulfate
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.00251
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17°C
0.0375
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
localization is suggested by an in vitro chloroplast import assay
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in Arabidopsis thaliana, the enzyme is essential for reproductive viability
malfunction
-
the apk1 apk3 apk4 triple mutant combination is pollen lethal
physiological function
-
the enzyme is essential for plant reproduction and viability
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APK1_ARATH
276
0
29787
Swiss-Prot
Chloroplast (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 1517.5% (w/v) PEG 2000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
additional information
-
the N-terminal truncation variant (APSKDELTA96) is completely insensitive to substrate inhibition by adenosine 5-phosphosulfate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme is rapidly inactivated by dialysis, dilution or freezing even in the presence of glycerol
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
-70°C, recombinant APS kinase fusion protein, 1 year, no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography and Superdex-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli as fusion protein with glutathione-S-transferase or maltose binding protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, S.; Leustek, T.
APS kinase from Arabidopsis thaliana: genomic organization, expression, and kinetic analysis of the recombinant enzyme
Biochem. Biophys. Res. Commun.
247
171-175
1998
Arabidopsis thaliana (Q43295), Arabidopsis thaliana
Lillig, C.H.; Schiffmann, S.; Berndt, C.; Berken, A.; Tischka, R.; Schwenn, J.D.
Molecular and catalytic properties of Arabidopsis thaliana adenylyl sulfate (APS)-kinase
Arch. Biochem. Biophys.
392
303-310
2001
Arabidopsis thaliana (O49196), Arabidopsis thaliana
Mugford, S.; Matthewman, C.; Hill, L.; Kopriva, S.
Adenosine-5'-phosphosulfate kinase is essential for Arabidopsis viability
FEBS Lett.
584
119-123
2010
Arabidopsis thaliana
Zhang, M.; Ravilious, G.E.; Hicks, L.M.; Jez, J.M.; McCulla, R.D.
Redox switching of adenosine-5-phosphosulfate kinase with photoactivatable atomic oxygen precursors
J. Am. Chem. Soc.
134
16979-16982
2012
Arabidopsis thaliana
Ravilious, G.E.; Jez, J.M.
Nucleotide binding site communication in Arabidopsis thaliana adenosine 5-phosphosulfate kinase
J. Biol. Chem.
287
30385-30394
2012
Arabidopsis thaliana (Q43295), Arabidopsis thaliana
Ravilious, G.E.; Westfall, C.S.; Jez, J.M.
Redox-linked gating of nucleotide binding by the N-terminal domain of adenosine 5-phosphosulfate kinase
J. Biol. Chem.
288
6107-6115
2013
Arabidopsis thaliana
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