| glucosylglycerol-phosphate phosphatase | <enzyme> Isolated from synechocystis; do not confuse with stpa protein from e. Coli Registry number: EC 3.1.3.- Synonym: stpa gene product, synechocystis (26 Jun 1999) |
|---|---|
| glyceraldehyde 3-phosphate phosphatase | <enzyme> Groundnut enzyme converts glyceraldehyde 3-phosphate to glyceraldehyde Registry number: EC 3.1.3.- Synonym: glph phosphatase (26 Jun 1999) |
| glycogen synthase-d phosphatase | <enzyme> An enzyme that catalyses the conversion of phosphorylated, inactive glycogen synthase d to active dephosphoglycogen synthase I. Chemical name: (UDPglucose:glycogen 4-alpha-D-glucosyltransferase-D) phosphohydrolase Registry number: EC 3.1.3.42 (12 Dec 1998) |
| ceramide-activated protein phosphatase | <enzyme> Belongs to the heterotrimeric subfamily of the pp2a group of serine-threonine protein phosphatases; involved in ceramide-mediated signal transduction; inhibited by okadaic acid Registry number: EC 3.1.3.- Synonym: ceramide-stimulated phosphatase, capp (enzyme) (26 Jun 1999) |
| PEP protein tyrosine phosphatase | <enzyme> Pest - pro, glu, ser and thr; an intracellular ptpase expressed primarily by cells of haematopoietic origin; involved in regulating nuclear tyrosine phosphorylation; amino acid sequence has been determined Registry number: EC 3.1.3.- Synonym: pep ptpase, pest-enriched phosphatase, ptp-pest (26 Jun 1999) |
| Gomori's non-specific acid phosphatase stain | <technique> A method in which formalin-fixed frozen sections are incubated in a substrate containing sodium beta-glycerophosphate and lead nitrate at pH 5.0; the insoluble lead phosphate produced is treated with ammonium sulfide to give a black lead sulfide. (05 Mar 2000) |
| Gomori's non-specific alkaline phosphatase stain | <technique> A calcium-cobalt sulfide method using frozen sections or cold acetone-or formalin-fixed paraffin sections, plus sodium beta-glycerophosphate as a substrate at pH 9.0 to 9.5 with Mg++ as activator; calcium ions precipitate the liberated phosphate, cobalt salt replaces the calcium phosphate, and ammonium sulfide converts the product to a black cobalt sulfide. (05 Mar 2000) |
| RLK5-associated protein phosphatase | <enzyme> Associated with serine-threonine receptor-like kinase, rlk5; from arabidopsis thaliana; composed of 3 domains, an amino-terminal signal anchor, a kinase interaction domain and a type 2c protein phosphatase catalytic domain; mw 65 kD; genbank u09505 Registry number: EC 3.1.3.- Synonym: kapp, kinase-associated protein phosphatase (26 Jun 1999) |
| choline phosphatase | <enzyme> An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyses transphosphatidylation reactions. Chemical name: Phosphatidylcholine phosphatidohydrolase Registry number: EC 3.1.4.4 (12 Dec 1998) |
| RNA-tyrosine phosphatase | <enzyme> Hela cell enzyme which removes 5'-terminal protein from poliovirus RNA by breaking the tyrosine-phosphate bond between the above two entities Registry number: EC 3.1.4.- Synonym: uridylyl-(5'p-o)-tyrosine phosphodiesterase, y-pupnpde, tyrosine-RNA phosphatase, uridylylpolynucleotide-(5'p-o)-tyrosine phosphodiesterase (26 Jun 1999) |
| chromatin 3'-phosphatase-5'-hydroxy kinase | <enzyme> Hydrolyzes the 3'-phosphate end of a polynucleotide duplex followed by ATP-mediated phosphorylation of the 5'-oh end Registry number: EC 3.1.3.- Synonym: chromatin-phosphatase-hydroxykinase (26 Jun 1999) |
| phenylalanine hydroxylase phosphatase | <enzyme> Catalyses dephosphorylation of phosphorylated phenylalanine hydroxylase Registry number: EC 3.1.3.- Synonym: phe hydroxylase phosphatase (26 Jun 1999) |
| microtubule-associated protein-2 phosphatase | <enzyme> does not fit into any of the classes of protein phosphatases (types 1,2a,2b and 2c) involved in cellular regulation Registry number: EC 3.1.3.- Synonym: map-2 phosphatase (26 Jun 1999) |
| phosphatase | <enzyme> That hydrolyse phosphomonoesters. Acid phosphatases are specific for the single charged phosphate group and alkaline phosphatases for the double charged group. These specificities do not overlap. The phosphatases comprise a very wide range of enzymes including broad and narrow specificity members. Phosphoprotein phosphatases specifically de phosphorylate a particular protein and are essential if phosphorylation is to be used as a reversible control system. (31 Dec 1997) |
| phosphatase unit | See: Bodansky unit, King unit. (05 Mar 2000) |