2.7.1.25: adenylyl-sulfate kinase
This is an abbreviated version!
For detailed information about adenylyl-sulfate kinase, go to the full flat file.
Word Map on EC 2.7.1.25
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2.7.1.25
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chrysogenum
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sulfate-activating
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3'-phosphate
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sulphurylase
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2.7.7.4
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brachymorphic
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cysd
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molybdolysis
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spondyloepimetaphyseal
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atp-sulphurylase
- 2.7.1.25
- chrysogenum
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sulfate-activating
- 3'-phosphate
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sulphurylase
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2.7.7.4
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brachymorphic
- cysd
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molybdolysis
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spondyloepimetaphyseal
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atp-sulphurylase
Reaction
Synonyms
3'-phosphoadenosine 5'-phosphosulfate synthetase1, 3'-phosphoadenosine-5'-phosphosulfate synthetase, 5'-phosphoadenosine sulfate kinase, adenosine 5'-phosphosulfate kinase, adenosine 5'-phosphosulphate kinase, adenosine 5-phosphosulfate kinase, adenosine 5’-phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate 3'-phosphotransferase, adenosine-5'-phosphosulfate kinase, adenosine-5'-phosphosulfate-3'-phosphokinase, adenosine-5'phosphosulfate kinase, adenosine-5’-phosphosulfate kinase, adenylyl-sulfate kinase, adenylylsulfate 3'-phosphotransferase, adenylylsulfate kinase, adenylylsulphate kinase, APK, APK1, APK2, APK3, APK4, APS kinase, APS-kinase, APSK, APSK1, ATP adenosine-5'-phosphosulfate 3'-phosphotransferase, ATP sulfurylase-APS kinase, CysC, EhAPSK, EHI_179080, kinase, adenylylsulfate (phosphorylating), MgATP:APS 3'-phosphotransferase, More, MXAN3487, MXAN_3487, MXAN_RS16905, PAPS 2, PAPS synthase, PAPS synthetase, PAPSS, PAPSS 1, PAPSS1
ECTree
2.7.1.25 adenylyl-sulfate kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.25 - adenylyl-sulfate kinase
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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
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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
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-AmericanÂ’s subject, almost no effect of mutations when expressed in COS-1 or HEK293 cells
G427A
H425A
H428A
N426K
R333C
identified as naturally occurring mutation, R333C found exclusively in Caucasian-AmericanÂ’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
C541A
the mutant shows reduced activity compared to the wild type enzyme
C549A
the mutant shows increased activity compared to the wild type enzyme
K19R
C36A/C69A
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the mutant is not inhibited by oxidized glutathione and shows activity reduced to 71%
S107C
similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket
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
additional information
K19R
site-directed mutagenesis, the P-loop Lys is substituted by Arg. K19R is a kinase-dead point mutation, because the Lys residue in the P-loop is required for productive ATP binding and kinase activity
K19R
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site-directed mutagenesis, the P-loop Lys is substituted by Arg. K19R is a kinase-dead point mutation, because the Lys residue in the P-loop is required for productive ATP binding and kinase activity
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additional information
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the N-terminal truncation variant (APSKDELTA96) is completely insensitive to substrate inhibition by adenosine 5Â’-phosphosulfate
additional information
the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
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the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
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generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
additional information
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construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
additional information
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construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
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