High impact information on NSC84663

• 3-Hydroxyaspartic acid and 3-hydroxyasparagine are two rare amino acids that are present in domains homologous to the epidermal growth factor precursor in vitamin K-dependent plasma proteins as well as in proteins that do not require vitamin K for normal biosynthesis [1].
• beta-Hydroxyaspartic acid in vitamin K-dependent protein C [2].
• Calcium binding to the isolated beta-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X [3].
• The light chain contains 0.2-0.3 mol of beta-hydroxyaspartic acid/mol of protein, indicating that an aspartic acid residue in bovine factor VII is incompletely hydroxylated [4].
• It has beta-hydroxyaspartic acid in position 71 which is in the first of its two domains that are homologous to epidermal growth factor (EGF) [5].

Biological context of NSC84663

• Acid hydrolysis of protein C released approximately equal to 1 mol of beta-hydroxyaspartic acid per mol of protein [2].
• A residue tentatively identified as beta-hydroxyaspartic acid [Arlaud, Willis & Gagnon (1986) Biochem. J., in the press] located in the C1r A-chain, within an epidermal-growth-factor consensus sequence, was found to be encoded as asparagine [6].
• Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid [7].
• The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens [8].
• Equilibrium dialysis experiments demonstrated that Gla-domainless human factor IXa beta retained two high-affinity calcium binding sites (Kd=52 microM), a finding essentially identical to that observed for Gla-domainless bovine factor IX that contains 0.8-0.9 moles of beta-hydroxyaspartic acid per mole of protein [9].

Associations of NSC84663 with other chemical compounds

• After hydrolysis in 6 M HCl, the beta-hydroxyaspartic acid released is quantitated on an automatic amino acid analyzer employing a pH 2.0 eluting buffer and postcolumn reaction with o-phthalaldehyde for detection [10].
• The non-selective EAAT inhibitor threo-beta-hydroxyaspartate had a significantly greater maximal inhibitory effect than did the EAAT2-selective inhibitor, dihydrokainate, indicating uptake by both EAAT2 and EAAT3 [11].
• The vitamin K-dependent plasma proteins were isolated from normal and scorbutic guinea pig plasma by barium citrate adsorption and the beta- hydroxyaspartic acid content was determined [12].
• To localize beta-hydroxyaspartic acid in factor IX and factor X the two proteins were cleaved with cyanogen bromide and trypsin, respectively [13].

Gene context of NSC84663

• What role does beta-hydroxyaspartic acid play in protein C activation and function [14]?
• Among vitamin K-dependent proteins, factor IX, factor X, protein C, and protein Z each contain about one residue of beta-hydroxyaspartic acid whereas protein S contains two or three residues [10].
• Prothrombin lacks beta-hydroxyaspartic acid as do a number of non-vitamin K-dependent proteins also analyzed [10].

References