词条 | Adenylyl-sulfate kinase |
释义 |
| 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 studiesAs 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}}. References1. ^{{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
3 : Protein domains|EC 2.7.1|Enzymes of known structure |
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