Fungi acid phosphatase

Purple acid phosphatase (PAP) or tartrate-resistant phosphatase is not thought to be a protein phosphatase but it has a very similar dimetallic active site structure to that found in protein phosphatases. PAPs have been identified in bacteria, plants, mammals, and fungi. The molecular weights (animal 35 kDa, plant 55 kDa) are different and they exhibit low sequence homology between kingdoms but the residues involved in coordination of the metal ions are invariant. " There has been considerable debate as to the identity of the metal ions in PAPs in vivo. Sweet potato, Ipomoea batatas, has been shown to possess two different PAP enzymes and the active site of one of them has been shown to contain one Fe and one Zn " " ion. Another report has established that the active site of a PAP from sweet potato contains one Fe " and one Mn +. The well-characterized red kidney bean enzyme and the soybean enzyme contain Fe " and Zn. Claims that PAP from sweet potato has 2Fe ions or 2Mn ions have been discussed elsewhere. One explanation is that these are different forms of the enzyme, another is that because the metal ions are labile and are rapidly incorporated into the active site, the enzyme contains a mixture of metal ions in vivo and the form isolated depends on the conditions of isolation. 

The lysosomes are the cell s stomach, serving to break down various cell components. For this purpose, they contain some 40 different types of hydrolases, which are capable of breaking down every type of macromolecule. The marker enzyme of lysosomes is acid phosphatase. The pH optimum of lysosomal enzymes is adjusted to the acid pH value and is also in the range of pH 5. At neutral pH, as in the cytoplasm, lysosomal enzymes only have low levels of activity. This appears to be a mechanism for protecting the cells from digesting themselves in case lysosomal enzymes enter the cytoplasm at any time. In plants and fungi, the cell vacuoles (see p. 43) have the function of lysosomes. 

The pioneering crystallization smdies on prostatic acid phosphatase and mammalian tartrate-resistant acid phosphatase conformed significant milestones towards the elucidation of the mechanisms followed by these enzymes (Schneider et al., EMBO J 12 2609-2615, 1993). Acid phosphatases are also found in nonmammalian species such as bacteria, fungi, parasites, and plants, and most of them share structural similarities with mammalian acid phosphatase enzymes. 

The third most important nutrient phosphorous is taken up from the environment as orthophosphate. Phosphorous are generally strongly bound to compounds in the environment. It can be as phosphate containing organics or as insoluble salts in the soil or present as minerals in rocks. Fungi use extracellular phosphatases to liberate phosphorous from organics. They also produce organic acids to dissolve insoluble salts and rocks to be able to take up phosphorous. 

G uany l-3,5-dimethy l-pyrazole nitrate Fungi (Mold), Yeast Amino acid oxidase, Aspergillus oryzae enzyme, Chymotrypsin, Diastase, Emulsin, Hexokinase, Hog kidney enzyme, Iso-merase. Papain, Phosphatase, Pseudo monas extract... 

Plant secondary metabolites may inhibit specific enzymes, either in plants or in other species such as fungi or animals. In some cases, this appears to be the sole mode of action of the metabolite, whereas in others, enzyme inhibition forms part of a suite of effects. It must be noted, however, that the specificity and in vivo biological relevance of some findings remains questionable. An example of this is the inhibition of a variety of enzymatic reactions, including plant hormone biosynthetic enzymes, catalase, maltase and phosphatase by phenolics and phenolic acids (Macias et al, 2007). 

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