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).
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
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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).
involved in the synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, inactivating mutations of PAPSS2 causes skeletal disorders
involved in the synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, inactivating mutations of PAPSS2 causes skeletal disorders
Characterization of Entamoeba histolytica adenosine 5'-phosphosulfate (APS) kinase; validation as a target and provision of leads for the development of new drugs against amoebiasis.
Characterization of Entamoeba histolytica adenosine 5'-phosphosulfate (APS) kinase; validation as a target and provision of leads for the development of new drugs against amoebiasis.
Discovery of Carbohydrate Sulfotransferase Inhibitors from a Kinase-Directed Library We thank Sharon Long and Dave Keating for providing both the NodH sulfotransferase and APS Kinase during our preliminary experiments and Jack Kirsch for numerous helpful conversations. J.I.A. and K.G.B were supported by NIH Molecular Biophysics Training Grant (No. T32GM0895). This research was funded by grants to C.R.B. from the Pew Scholars Program, the W. M. Keck Foundation and the American Cancer Society (Grant No. RPG9700501BE).
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
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
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
identified as naturally occurring mutation, E531Q found in a single sample of an African-Americans subject, almost no effect of mutations when expressed in COS-1 or HEK293 cells
identified as naturally occurring mutation, R333C found exclusively in Caucasian-Americans DNA, almost no effect of mutations when expressed in COS-1 or HEK293 cells
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
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
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
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
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
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
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
Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains
Structural mechanism for substrate inhibition of the adenosine 5-phosphosulfate kinase domain of human 3-phosphoadenosine 5-phosphosulfate synthetase 1 and its ramifications for enzyme regulation
J. Biol. Chem.
282
22112-22121
2007
Homo sapiens (O43252), Homo sapiens (O95340), Homo sapiens