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Gene Review

ECs3604  -  adenylylsulfate kinase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs3604


High impact information on ECs3604

  • The cumulative results indicate that Ser-107 may reside in the substrate binding pocket of fungal APS kinase, but neither it nor any nearby hydroxy amino acid serves as an obligatory phophoryl acceptor in the 3'-phosphoadenylylsulfate synthesis reaction [3].
  • Replacement of Ser-107 with alanine yielded an active enzyme with kinetic characteristics similar to those of wild-type APS kinase [3].
  • The results also indicate that the absence of a serine at position 478 in the APS kinase-like C-terminal region of fungal ATP sulfurylase does not account for the lack of APS kinase activity in that enzyme [3].
  • The sequence includes the structural genes encoding the enzymes ATP sulfurylase (cysD and cysN) and APS kinase (cysC) which catalyze the synthesis of activated sulfate [4].
  • APS kinase catalyses the transfer of the gamma phosphoryl group of ATP to the 3'-hydroxyl group of APS [2].

Chemical compound and disease context of ECs3604


Biological context of ECs3604


Associations of ECs3604 with chemical compounds

  • The enzymes of the sulfate activation pathway, ATP sulfurylase (ATP:sulfate adenylyltransferase, EC and APS kinase (ATP:adenosine-5'-phosphosulfate 3'-phosphotransferase, EC have been overproduced approximately 100-fold [6].
  • APS kinase binds one Mn(2+) ion per subunit in the absence of substrates, consistent with the requirement for a divalent cation in the phosphorylation of APS by E-P [7].
  • APS kinase requires divalent cations such as Mg(2+) or Mn(2+) for activity [7].


  1. 5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria. Williams, S.J., Senaratne, R.H., Mougous, J.D., Riley, L.W., Bertozzi, C.R. J. Biol. Chem. (2002) [Pubmed]
  2. The ORF1 of the gentamicin-resistance operon (aac) of Pseudomonas aeruginosa encodes adenosine 5'-phosphosulphate kinase. Satishchandran, C., Taylor, J.C., Markham, G.D. Mol. Microbiol. (1993) [Pubmed]
  3. Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues. MacRae, I.J., Rose, A.B., Segel, I.H. J. Biol. Chem. (1998) [Pubmed]
  4. The DNA sequence of the sulfate activation locus from Escherichia coli K-12. Leyh, T.S., Vogt, T.F., Suo, Y. J. Biol. Chem. (1992) [Pubmed]
  5. Characterization of the phosphorylated enzyme intermediate formed in the adenosine 5'-phosphosulfate kinase reaction. Satishchandran, C., Hickman, Y.N., Markham, G.D. Biochemistry (1992) [Pubmed]
  6. The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization. Leyh, T.S., Taylor, J.C., Markham, G.D. J. Biol. Chem. (1988) [Pubmed]
  7. Mechanistic studies of Escherichia coli adenosine-5'-phosphosulfate kinase. Satishchandran, C., Markham, G.D. Arch. Biochem. Biophys. (2000) [Pubmed]
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