Adenylyl-sulfate kinase

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adenylylsulfate kinase
3cr8.jpg
Adenylylsulfate kinase homohexamer, Thiobacillus denitrificans
Identifiers
EC no. 2.7.1.25
CAS no. 9012-38-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins
APS_kinase
PDB 1m8p EBI.jpg
crystal structure of p. chrysogenum atp sulfurylase in the t-state
Identifiers
SymbolAPS_kinase
Pfam PF01583
Pfam clan CL0023
InterPro IPR002891
SCOP2 1d6j / SCOPe / SUPFAM
CDD cd02027
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, an adenylyl-sulfate kinase (EC 2.7.1.25) is an enzyme that catalyzes the chemical reaction

Contents

ATP + adenylyl sulfate ADP + 3'-phosphoadenylyl sulfate

Thus, the two substrates of this enzyme are ATP and adenylyl sulfate, whereas its two products are ADP and 3'-phosphoadenylyl sulfate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:adenylyl-sulfate 3'-phosphotransferase. Other names in common use include adenylylsulfate kinase (phosphorylating), 5'-phosphoadenosine sulfate kinase, adenosine 5'-phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate-3'-phosphokinase, and APS kinase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.

This enzyme contains an ATP binding P-loop motif. [1]

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1D6J, 1M7G, 1M7H, 1X6V, 1XJQ, 1XNJ, 2AX4, 2GKS, 2OFW, 2OFX, and 2PEY.

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References

  1. MacRae IJ, Rose AB, Segel IH (October 1998). "Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues". J. Biol. Chem. 273 (44): 28583–9. doi: 10.1074/jbc.273.44.28583 . PMID   9786849.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR002891