Adenylyl-sulfate kinase explained

adenylylsulfate kinase
Ec Number:	2.7.1.25
Cas Number:	9012-38-8
Go Code:	0004020
Width:	270

Symbol:	APS_kinase
APS_kinase
Pfam:	PF01583
Pfam Clan:	CL0023
Interpro:	IPR002891
Scop:	1d6j
Cdd:	cd02027

In enzymology, an adenylyl-sulfate kinase is an enzyme that catalyzes the chemical reaction

ATP + adenylyl sulfate

\rightleftharpoons 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,,,,,,,,,, and .

Further reading

• Bandurski RS, Wilson LG, Squires CL . 1956 . The mechanism of "active sulfate" formation . J. Am. Chem. Soc. . 78 . 6408 - 6409 . 10.1021/ja01605a028 . 24 .
• ROBBINS PW, LIPMANN F . 1957 . Isolation and identification of active sulfate . J. Biol. Chem. . 229 . 837 - 51 . 13502346 . 2 .
• Venkatachalam KV, Akita H, Strott CA . 1998 . Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains . J. Biol. Chem. . 273 . 19311 - 20 . 9668121 . 10.1074/jbc.273.30.19311 . 30 . free .

Notes and References

1. MacRae IJ, Rose AB, Segel IH . 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 . October 1998. 9786849 . 10.1074/jbc.273.44.28583. free .