Examples of aspartate

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In some cases the one-letter abbreviations for certain amino acids have been added to distinguish between, for example, aspartate and glutamate.
Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteins.
Abnormal liver biochemistry was defined as at least one abnormal value of alanine aminotransferase, aspartate aminotransferase, gamma-glutamyl-transpeptidase and total bilirubin.
The most frequent amino acid whose sidechain is contacting the magnesium ion is aspartate (42 %), followed by threonine (23 %), glutamate (17 %) and serine (10 %).
In both cases negatively charged glutamate and aspartate residues are critical for binding.
Sonicates of mitochondria enriched in astrocytes had 50% less aspartate aminotransferase than control mitochondria, but citrate synthase was the same in the two preparations.
This residue is highly conserved throughout the species, and replacement by an aspartate residue would be predicted to impair cofactor binding.
The aspartate aminotransferase, alanine aminotransferase, gamma-glutamyl transpeptidase, leukocyte and neutrophil values of infected lambs increased, but those of lymphocytes decreased.
Interestingly, an active-site aspartate residue has been identified in both instances, which is relevant for catalysis, although with distinct putative roles.
Surprisingly, only 8 % of the contacts are to glutamate, so there seems to be a strong preference for aspartate over glutamate.
These reactions involve the transfer of the amino group from aspartate, alanine, leucine, or ornithine to a-ketoglutarate to produce glutamate.
The typical response regulator comprises a regulatory domain that includes a phosphorylatable aspartate residue and an associated effector domain, often a transcription factor.
Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.
The ribose oxygens preferentially interact with mainchain atoms (39 %, 31 % of which are glycines) followed by arginine\\lysine and aspartate\\glutamate.
Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion.
Results of two extensive studies - on ribosomes and on the allosteric protein aspartate transcarbamoylase - illustrate the application of the various methods.
Substrate modification, particularly by the addition of amino acids such as aspartate and glutamate, have been shown to be of benefit as well.

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