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  2. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    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 ...

  3. Histidine phosphotransfer domain - Wikipedia

    en.wikipedia.org/wiki/Histidine_phosphotransfer...

    The histidine phosphotransfer function can be carried out by proteins with at least two different architectures, both composed of a four-helix bundle but differing in the way the bundle is assembled. Most structurally characterized HPt proteins, such as the Hpt domain from the Escherichia coli protein ArcB and the Saccharomyces cerevisiae ...

  4. Essential amino acids in plant food - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acids_in...

    In case of humans there are 9 EAAs: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. [1] EAAs are provided in both animal and plant-based food. The EAAs in plants vary greatly due to the vast variation in the plant world and, in general, plants have much lower content of proteins than animal ...

  5. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    This leader sequence is important for the regulation of histidine in E. coli. The His operon operates under a system of coordinated regulation where all the gene products will be repressed or depressed equally. The main factor in the repression or derepression of histidine synthesis is the concentration of histidine charged tRNAs.

  6. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    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 ...

  7. Ribose-phosphate diphosphokinase - Wikipedia

    en.wikipedia.org/wiki/Ribose-phosphate...

    The enzyme is involved in the synthesis of nucleotides (purines and pyrimidines), cofactors NAD and NADP, and amino acids histidine and tryptophan, [1] [2] [3] linking these biosynthetic processes to the pentose phosphate pathway, from which the substrate ribose 5-phosphate is derived.

  8. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    In plants, the shikimate pathway first leads to the formation of chorismate, which is the precursor of phenylalanine, tyrosine, and tryptophan. These aromatic amino acids are the precursors of many secondary metabolites, all essential to a plant's biological functions, such as the hormones salicylate and auxin. This pathway contains enzymes ...

  9. Laccase - Wikipedia

    en.wikipedia.org/wiki/Laccase

    The type I copper does not bind O 2, but functions solely as an electron transfer site. The type I copper center consists of a single copper atom that is ligated to a minimum of two histidine residues and a single cysteine residue, but in some laccases produced by certain plants and bacteria, the type I copper center contains an additional ...