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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 ...
The endothelial protease vasohibin [f] uses a cysteine as the nucleophile, but a serine to coordinate the histidine base. [43] [44] Despite the serine being a poor acid, it is still effective in orienting the histidine in the catalytic triad. [43] Some homologues alternatively have a threonine instead of serine at the acid location. [43]
In 1999, Chul-Ho Jun and Hyuk Lee reported the first example of hydroacylation through shuttle catalysis. [5] In this example, 3-methyl-2-aminopyridine was used to activate the acyl group as well as coordinate to the rhodium catalyst, promoting C–C bond cleavage to eventually enable aldehyde transfer from a ketone to an alkene.
Histidine-tryptophan-ketoglutarate, or Custodiol HTK solution, is a high-flow, low-potassium preservation solution used for organ transplantation. The solution was initially developed by Hans-Jürgen Bretschneider.
In enzymology, a protein-histidine N-methyltransferase (EC 2.1.1.85) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + protein L-histidine ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
In enzymology, a protein-histidine pros-kinase (EC 2.7.13.1) is an enzyme that catalyzes the chemical reaction. ATP + protein L-histidine ADP + protein N π-phospho-L-histidine. Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein Npi-phospho-L-histidine.
The two main systems in humans are the glycerol phosphate shuttle and the malate-aspartate shuttle. The malate/a-ketoglutarate antiporter functions move electrons while the aspartate/glutamate antiporter moves amino groups. This allows the mitochondria to receive the substrates that it needs for its functionality in an efficient manner. [1]
Protons tunnel across a series of hydrogen bonds between hydronium ions and water molecules.. The Grotthuss mechanism (also known as proton jumping) is a model for the process by which an 'excess' proton or proton defect diffuses through the hydrogen bond network of water molecules or other hydrogen-bonded liquids through the formation and concomitant cleavage of covalent bonds involving ...