phosphatase

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phosphatase

 [fos´fah-tās]
any of a group of enzymes capable of catalyzing the hydrolysis of esterified phosphoric acid, with liberation of inorganic phosphate, found in practically all tissues, body fluids, and cells, including erythrocytes and leukocytes.
acid phosphatase see acid phosphatase.
alkaline phosphatase see alkaline phosphatase.

phos·pha·tase

(fos'fă-tās),
Any of a group of enzymes (EC 3.1.3.x) that liberate orthophosphate from phosphoric esters.
See also: phosphohydrolases.

phosphatase

/phos·pha·tase/ (-tās) any of a group of enzymes that catalyze the hydrolytic cleavage of inorganic phosphate from esters.

phosphatase

(fŏs′fə-tās′, -tāz′)
n.
Any of numerous enzymes that catalyze the removal of phosphate groups by hydrolysis of phosphate ester bonds. They act in the opposite manner to kinases and are important in metabolism and cell signaling.

phosphatase

[fos′fətāz]
an enzyme that acts as a catalyst in chemical reactions involving phosphorus. It is present in serum, semen, the kidney, and the prostate. It is essential in the calcification of bone. See also catalyst, enzyme.

phos·pha·tase

(fos'fă-tās)
Any of a group of enzymes (EC sub-subclass 3.1.3) that liberate inorganic phosphate from phosphoric esters.

phosphatase

An enzyme that removes phosphate groups from a molecule.

phosphatase

an enzyme that catalyses the release of phosphate from a molecule. For example, in the mammalian liver phosphorylated glucose can be broken down to glucose with a phosphatase enzyme. see GLYCOGEN.

phos·pha·tase

(fos'fă-tās)
Any of a group of enzymes (EC sub-subclass 3.1.3) that liberate inorganic phosphate from phosphoric esters.

phosphatase(s) (fos´fətās),

n a group of enzymes that are distributed throughout most cells and body fluids and are characterized by their ability to hydrolyze a wide variety of monophosphate esters to alcohols and inorganic phosphate.
phosphatase, acid,
n a group of phosphatases (e.g., serum, liver, prostate) with optimal activity below a pH level of 7. Elevated serum levels have been observed in metastatic breast and prostatic cancer; Paget's, Gaucher's, and Niemann-Pick diseases and in myelocytic leukemia.
phosphatase, alkaline,
n a group of phosphatases (e.g., serum, liver, bone) whose optimal activity ranges near a pH level of 9.8. Elevated blood levels occur in Paget's disease and pregnancy, whereas low levels are characteristic of dwarfism and a generalized nutritional protein deficiency.

phosphatase

any of a group of enzymes capable of catalyzing the hydrolysis of esterified phosphoric acid, with liberation of inorganic phosphate, found in practically all tissues, body fluids and cells, including erythrocytes and leukocytes.

acid phosphatase
a lysosomal enzyme that hydrolyzes phosphate esters liberating phosphate, showing optimal activity at a pH between 3 and 6; found in erythrocytes, prostatic tissue, spleen, kidney and other tissues.
alkaline phosphatase
an isoenzyme showing optimal activity at a pH of about 10; found in bone, liver, kidney, leukocytes, adrenal cortex and other tissues, often used in clinical diagnosis of liver and/or bone damage. Called also AP; see also alkaline phosphatase.
phosphatase inhibitor-1
inhibitor of phosphatase enzymes known to activate glycogen synthesis or inactivate glycogen breakdown. Need to themselves be phosphorylated by cAMP-dependent kinases before they are effective in their inhibitory activity.
References in periodicals archive ?
Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A.
So they concluded that these compounds displayed their main mechanism of insecticidal activity after they inhibited protein serine/threonine phosphatases activity in P.
Quantification of liver alkaline phosphatase isoenzyme activity using heat inactivation and phenylalanine inhibition techniques: Comparison of two methods.
The Src homology 2 domain-containing protein tyrosine phosphatase-2 (SHP-2), characterized by two N-terminal Src homology 2 domains, a central catalytic domain and a C-terminal protein tyrosine phosphatase (PTP) domain, is an evolutionarily conserved intracellular PTP.
The present study was conducted to evaluate the effect of buctril super herbicide on soil bacteria, fungi and actinomycetes population and also on soil urease, dehydrogenase and alkaline phosphatase activity.
Our experiments suggest that root phosphatases are a contributing factor.
Prenylation-dependent association of protein-tyrosine phosphatases PRL-1,-2, and-3 with the plasma membrane and the early endosome.
The effects of pisiferdiol having a unique seven-membered ring on protein phosphatases are more specific than pisiferic acid having a normal six-membered ring, and our data provide the first evidence that pisiferdiol specifically activates PP2C in vitro and in vivo.
Serum alkaline phosphatase, calcium and phosphorus, and magnesium levels were measured in 23 skiers, 21 runners, 24 wrestlers, 20 handball, 21 soccers and 30 sedentary living healthy individual.
Consequently, studies that contribute to a better understanding of the role of acid phosphatases in plants are of particular importance.