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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 protonated), classifying it as a ...
Histidine phosphotransfer domains and histidine phosphotransferases (both often abbreviated HPt) are protein domains involved in the "phosphorelay" form of two ...
The glycerol phosphate shuttle was first characterized as a major route of mitochondrial hydride transport in the flight muscles of blow flies. [5] [6] It was initially believed that the system would be inactive in mammals due to the predominance of lactate dehydrogenase activity over glycerol-3-phosphate dehydrogenase 1 (GPD1) [5] [7] until high GPD1 and GPD2 activity were demonstrated in ...
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.
The OH group in the active site acts as a nucleophile to attack the phosphorus in DIFP and form a tetrahedral intermediate and release a proton. Then the P-F bond is broken, one electron is transferred to the F atom and it leaves the intermediate as F − anion. It combines with a proton in solution to form one HF molecule.
Taken together, import of ADP and Pi and export of the resulting ATP results in one proton imported, subtracting from the number available for use by the ATP synthase directly. Taking this into account, it takes 8/3 +1 or 3.67 protons for vertebrate mitochondria to synthesize one ATP in the cytoplasm from ADP and Pi in the cytoplasm.
The autophosphorylation H-box is contained in the N-terminal dimerization and histidine phosphotransfer (DHp) domain. In HK853-CD, crystallized from Thermotoga maritima, this domain is a helical-hairpin and is formed by residues 232-317. The histidine phosphorylation site is located at His-260.
HRG is a glycoprotein of 70-75kDa present at a relatively high concentration in the plasma of vertebrates.The primary structure of human HRG is predicted to be a 507 amino acid multidomain polypeptide consisting of two cystatin-like regions at the N-terminus, a histidine-rich region (HRR) flanked by proline-rich regions (PRR), and a C-terminal domain. [10]