Difference between revisions of "Phosphatase Subfamily PGP"
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[[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
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- Error fetching PMID 24338687:
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