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Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...
Histidinemia is a rare autosomal recessive metabolic disorder caused by a deficiency of the enzyme histidase. Histidase is needed for the metabolism of the amino acid histidine . [ 1 ] Although originally thought to be linked to multiple developmental disorders histidinemia is now accepted as a relatively benign disorder, [ 2 ] leading to a ...
The use of acidosis for a low pH creates an ambiguity in its meaning. The difference is important where a patient has factors causing both acidosis and alkalosis, wherein the relative severity of both determines whether the result is a high, low, or normal pH. [citation needed] Alkalemia occurs at a pH over 7.45.
The triad of cytomegalovirus protease [b] uses histidine as both the acid and base triad members. Removing the acid histidine results in only a 10-fold activity loss (compared to >10,000-fold when aspartate is removed from chymotrypsin). This triad has been interpreted as a possible way of generating a less active enzyme to control cleavage ...
An abnormally low pH in the extracellular fluid is called an acidemia and an abnormally high pH is called an alkalemia. [citation needed] Acidemia and alkalemia unambiguously refer to the actual change in the pH of the extracellular fluid (ECF). [24] Two other similar sounding terms are acidosis and alkalosis. They refer to the customary effect ...
Histamine is derived from the decarboxylation of the amino acid histidine, a reaction catalyzed by the enzyme L-histidine decarboxylase. It is a hydrophilic vasoactive amine . Conversion of histidine to histamine by histidine decarboxylase
Histidine and aspartate phosphorylation occurs in prokaryotes as part of two-component signaling and in some cases in eukaryotes in some signal transduction pathways. The analysis of phosphorylated histidine using standard biochemical and mass spectrometric approaches is much more challenging than that of Ser, Thr or Tyr.
Lactic acidosis is commonly found in people who are unwell, such as those with severe heart and/or lung disease, a severe infection with sepsis, the systemic inflammatory response syndrome due to another cause, severe physical trauma, or severe depletion of body fluids. [3]