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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    The pH of the intracellular fluid and the extracellular fluid need to be maintained at a constant level. [ 2 ] The three dimensional structures of many extracellular proteins, such as the plasma proteins and membrane proteins of the body's cells , are very sensitive to the extracellular pH.

  4. Alkaline phosphatase - Wikipedia

    en.wikipedia.org/wiki/Alkaline_phosphatase

    The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic ...

  5. Nitrate reductase - Wikipedia

    en.wikipedia.org/wiki/Nitrate_reductase

    The very last step of nitrate reductase inactivation is the binding of the 14-3-3 adapter protein, which is initiated by the presence of Mg 2+ and Ca 2+. [14] Higher plants and some algae post-translationally regulate NR by phosphorylation of serine residues and subsequent binding of a 14-3-3 protein. [15]

  6. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. [3] The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. [4] [5] These phosphorylations play important and well-characterized roles in signaling pathways and metabolism.

  7. Acid phosphatase - Wikipedia

    en.wikipedia.org/wiki/Acid_phosphatase

    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 .

  8. Ribonuclease - Wikipedia

    en.wikipedia.org/wiki/Ribonuclease

    Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.

  9. Trehalase - Wikipedia

    en.wikipedia.org/wiki/Trehalase

    Since then the trehalose hydrolyzing enzyme, trehalase (α, α-trehalose-1-C-glucohydrolase, EC 3.2.1.28) has been reported from many other organisms including plants and animals. [6] Though trehalose is not known to be produced by mammals, trehalase enzyme is found to be present in the kidney brush border membrane and the intestinal villi ...