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词条 Adenylyl-sulfate kinase
释义

  1. Structural studies

  2. References

  3. Further reading

{{enzyme
| Name = adenylylsulfate kinase
| EC_number = 2.7.1.25
| CAS_number = 9012-38-8
| IUBMB_EC_number = 2/7/1/25
| GO_code = 0004020
| image =
| width =
| caption =
}}{{Infobox protein family
| Symbol = APS_kinase
| Name = APS_kinase
| image = PDB 1m8p EBI.jpg
| width =
| caption = crystal structure of p. chrysogenum atp sulfurylase in the t-state
| Pfam = PF01583
| Pfam_clan = CL0023
| InterPro = IPR002891
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1d6j
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD = cd02027
}}

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

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 {{PDB link|1D6J}}, {{PDB link|1M7G}}, {{PDB link|1M7H}}, {{PDB link|1X6V}}, {{PDB link|1XJQ}}, {{PDB link|1XNJ}}, {{PDB link|2AX4}}, {{PDB link|2GKS}}, {{PDB link|2OFW}}, {{PDB link|2OFX}}, and {{PDB link|2PEY}}.

References

1. ^{{cite journal | vauthors = MacRae IJ, Rose AB, Segel IH | title = Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues | journal = J. Biol. Chem. | volume = 273 | issue = 44 | pages = 28583–9 |date=October 1998| pmid = 9786849 | doi = 10.1074/jbc.273.44.28583| url = }}

Further reading

  • {{cite journal | vauthors = Bandurski RS, Wilson LG, Squires CL | date = 1956 | title = The mechanism of "active sulfate" formation | journal = J. Am. Chem. Soc. | volume = 78 | pages = 6408–6409 | doi = 10.1021/ja01605a028 | issue = 24 }}
  • {{cite journal | vauthors = ROBBINS PW, LIPMANN F | date = 1957 | title = Isolation and identification of active sulfate | journal = J. Biol. Chem. | volume = 229 | pages = 837–51 | pmid = 13502346 | issue = 2 }}
  • {{cite journal | vauthors = Venkatachalam KV, Akita H, Strott CA | date = 1998 | title = Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains | journal = J. Biol. Chem. | volume = 273 | pages = 19311–20 | pmid = 9668121 | doi = 10.1074/jbc.273.30.19311 | issue = 30 }}
{{Kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{InterPro content|IPR002891}}{{2.7-enzyme-stub}}

3 : Protein domains|EC 2.7.1|Enzymes of known structure

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