aspartic acid oor Katalaans
aspartic acid
en
(biochemistry) A nonessential amino acid, L-α-amino-succinic acid, (C <sub>4</sub> H <sub>7</sub> NO <sub>4</sub> ), found in animal protein and in sugar beet etc.
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Along with histidine 57 and aspartic acid 102, this serine residue constitutes the catalytic triad of the active site.
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The ionic charges of mucin are mainly provided by acidic amino acids including aspartic acid (pKa=3.9) and glutamic acid (pKa=4.2).
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The N5-MeTHF binding domain contains a conserved barrel in which N5-MeTHF can hydrogen bond with asparagine, arginine, and aspartic acid residues.
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The cream locus is on exon 2 of the MATP gene; a single nucleotide polymorphism results in an aspartic acid-to-asparagine substitution (N153D).
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Aspartic acid, for example, has a negative side chain when the pH value is above 3.9, while a neutrally charged side chain will be introduced as pH value drops below 3.9.
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An acidic amino acid features in the integrin-interaction site of many ECM proteins, for example as part of the amino acid sequence Arginine-Glycine-Aspartic acid ("RGD" in the one-letter amino acid code).
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However, a kind of bacteria, Helicobacter pylori, is prone to producing base to elevate the pH value in stomach, leading to the deprotonation of aspartic acids and glutamic acids, i.e., from neutral to negative-charged.
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This letter system was defined by the IUPAC and IUBMB in 1983, and is as follows: K—Lysine D—Aspartic acid E—Glutamic acid L—Leucine Therefore, the KDEL sequence in three letter code is: Lys-Asp-Glu-Leu.
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The specific set of reactions differs among organisms, but a common feature is the generation of quinolinic acid (QA) from an amino acid—either tryptophan (Trp) in animals and some bacteria, or aspartic acid (Asp) in some bacteria and plants.
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In the first reaction unique to purine nucleotide biosynthesis, PPAT catalyzes the displacement of PRPP's pyrophosphate group (PPi) by an amide nitrogen donated from either glutamine (N), glycine (N&C), aspartate (N), folic acid (C1), or CO2.
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The amino acid side-chains glutamic acid 35 (Glu35) and aspartate 52 (Asp52) have been found to be critical to the activity of this enzyme.
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The second histidine is not as effective an acid as the more common aspartate or glutamate, leading to a lower catalytic efficiency.
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In similar fashion, proteins that have to bind to positively charged molecules have surfaces rich with negatively charged amino acids like glutamate and aspartate, while proteins binding to negatively charged molecules have surfaces rich with positively charged chains like lysine and arginine.
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Instead of uric acid secretion, guanine and IMP can be used for recycling purposes and nucleic acid synthesis in the presence of PRPP and aspartate (NH3 donor).
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Key enzymes that synthesize certain amino acids are not present in animals—such as aspartokinase, which catalyses the first step in the synthesis of lysine, methionine, and threonine from aspartate.
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Examples are as follows: Alanine + α-ketoglutarate ⇌ pyruvate + glutamate Aspartate + α-ketoglutarate ⇌ oxaloacetate + glutamate Both pyruvate and oxaloacetate are key components of cellular metabolism, contributing as substrates or intermediates in fundamental processes such as glycolysis, gluconeogenesis, and the citric acid cycle.
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