Difference between revisions of "Phosphatase Subfamily PGP"
From PhosphataseWiki
(→Function) |
|||
| Line 2: | Line 2: | ||
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_PGP|Subfamily PGP]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_PGP|Subfamily PGP]] | ||
| − | PGP is ubiquitous in eukaryotes | + | PGP is ubiquitous in eukaryotes and has been reported to act on both proteins and small molecules. |
=== Evolution === | === Evolution === | ||
| − | + | PGP is found in most eukaryotes, typically in a single copy. Vertebrates encode two members: PGP and PDXP. | |
=== Domain === | === Domain === | ||
| − | + | PGPs have a single HAD-fold domain. | |
| − | === | + | === Functions === |
PDXP (Chronophin) is abundantly expressed in brain <cite>Jang03</cite> (see also [http://www.gtexportal.org/home/gene/PDXP GTEx] RNA-seq data). PDXP has two distinct substrates. | PDXP (Chronophin) is abundantly expressed in brain <cite>Jang03</cite> (see also [http://www.gtexportal.org/home/gene/PDXP GTEx] RNA-seq data). PDXP has two distinct substrates. | ||
* Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis <cite>Gao94, Jang03, Kim05</cite>. | * Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis <cite>Gao94, Jang03, Kim05</cite>. | ||
| − | * | + | * Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>. [[Phosphatase_Subfamily_Slingshot|slingshot]], also dephosphorylates cofilin. |
| − | In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological | + | In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological substrates are unknown. It also has a conserved phosphoglycolate phosphatase activity. |
| − | + | The yeast PGP, PHO13, has serine phosphatase activity against histone II-A and casein <cite>Tuleva98</cite>, and also acts on the synthetic small-molecule substrate PNPP ([https://en.wikipedia.org/wiki/Para-Nitrophenylphosphate para-nitrophenyl phosphate]). Deletion of PHO13 increases expression of pentose phosphate pathway genes and allows more efficient use of xylose. | |
=== References === | === References === | ||
Revision as of 02:32, 22 March 2015
Phosphatase Classification: Fold HAD: Superfamily HAD: Family NagD: Subfamily PGP
PGP is ubiquitous in eukaryotes and has been reported to act on both proteins and small molecules.
Evolution
PGP is found in most eukaryotes, typically in a single copy. Vertebrates encode two members: PGP and PDXP.
Domain
PGPs have a single HAD-fold domain.
Functions
PDXP (Chronophin) is abundantly expressed in brain [1] (see also GTEx RNA-seq data). PDXP has two distinct substrates.
- Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis [1, 2, 3].
- Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments [4, 5, 6]. slingshot, also dephosphorylates cofilin.
In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also GTEx RNA-seq data). PGP is a putative tyrosine-specific phosphatase [7], but its physiological substrates are unknown. It also has a conserved phosphoglycolate phosphatase activity.
The yeast PGP, PHO13, has serine phosphatase activity against histone II-A and casein [8], and also acts on the synthetic small-molecule substrate PNPP (para-nitrophenyl phosphate). Deletion of PHO13 increases expression of pentose phosphate pathway genes and allows more efficient use of xylose.
References
- Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, and Kwon OS. Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J Biol Chem. 2003 Dec 12;278(50):50040-6. DOI:10.1074/jbc.M309619200 |
- Gao G and Fonda ML. Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes. J Biol Chem. 1994 Mar 18;269(11):8234-9.
- Kim DW, Eum WS, Choi HS, Kim SY, An JJ, Lee SH, Sohn EJ, Hwang SI, Kwon OS, Kang TC, Won MH, Cho SW, Lee KS, Park J, and Choi SY. Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies. J Biochem Mol Biol. 2005 Nov 30;38(6):703-8. DOI:10.5483/bmbrep.2005.38.6.703 |
- Gohla A, Birkenfeld J, and Bokoch GM. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol. 2005 Jan;7(1):21-9. DOI:10.1038/ncb1201 |
- Huang TY, Minamide LS, Bamburg JR, and Bokoch GM. Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Dev Cell. 2008 Nov;15(5):691-703. DOI:10.1016/j.devcel.2008.09.017 |
- Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, and Gohla A. Chronophin dimerization is required for proper positioning of its substrate specificity loop. J Biol Chem. 2014 Jan 31;289(5):3094-103. DOI:10.1074/jbc.M113.536482 |
- Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, and Gohla A. Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities. J Biol Chem. 2014 Feb 7;289(6):3416-31. DOI:10.1074/jbc.M113.503359 |
- Tuleva B, Vasileva-Tonkova E, and Galabova D. A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity. FEMS Microbiol Lett. 1998 Apr 1;161(1):139-44. DOI:10.1111/j.1574-6968.1998.tb12940.x |
