Structural highlights
Function
CYSQ_MYCTU Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo. Glucose-1-phosphate (G-1-P), p-nitrophenyl phosphate (pNPP), and beta-glycerol phosphate (beta-GP) are also good substrates, compared to I-1-P. With much lower efficiency, can also hydrolyze inositol 2-phosphate (I-2-P) and glucose-6-phosphate (G-6-P) in vitro, but not fructose-6-phosphate (F-6-P) and trehalose-6-phosphate (T-6-P).[1] [2]
See Also
References
- ↑ Gu X, Chen M, Shen H, Jiang X, Huang Y, Wang H. Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase. Biochem Biophys Res Commun. 2006 Jan 20;339(3):897-904. PMID:16325768 doi:10.1016/j.bbrc.2005.11.088
- ↑ Hatzios SK, Iavarone AT, Bertozzi CR. Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase. Biochemistry. 2008 May 27;47(21):5823-31. PMID:18454554 doi:10.1021/bi702453s
