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Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...
Works best at pH 8. Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro. Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. Heat stable. Pepsin - cuts before Leu, Phe, Trp or Tyr, unless preceded by Pro. Also others, quite nonspecific; works best at pH 2.
Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.
The optimum pH for its action is approximately 7. [10] Its concentration does not correlate with the amount of HCl or pepsin in the gastric juice, e.g., intrinsic factor may be present even when pepsin is largely absent. [11] The site of formation of the intrinsic factor varies in different species.
Studies of proteins adapted to low pH have revealed a few general mechanisms by which proteins can achieve acid stability. In most acid stable proteins (such as pepsin and the soxF protein from Sulfolobus acidocaldarius), there is an overabundance of acidic residues which minimizes low pH destabilization induced by a buildup of positive charge ...
Mucorpepsin (EC 3.4.23.23, Mucor rennin, Mucor aspartic proteinase, Mucor acid proteinase, Mucor acid protease, Mucor miehei aspartic proteinase, Mucor miehei aspartic protease, Mucor pusillus emporase, Fromase 100, Mucor pusillus rennin, Fromase 46TL, Mucor miehei rennin) is an enzyme.
Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase .