| glucogenic amino acid | <biochemistry> A type of amino acid with carbon chains that can be broken down into an intermediate of the citric acid cycle such as glycogen and then converted into glucose as a means of entering the normal process of carbohydrate metabolism in the body. Examples include: Glycine, alanine, arginine, and ornithine. (14 Oct 1997) |
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| RNA, transfer, amino acid-specific | A group of transfer rnas which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis. (12 Dec 1998) |
| polar amino acid | An alpha-amino acid in which the functional group attached to the alpha-carbon (i.e., R in RCH(NH2)COOH) has hydrophilic properties; e.g., serine, cysteine, homocysteine. (05 Mar 2000) |
| sequence homology, amino acid | The degree of similarity between sequences of amino acids. This information is useful for the understanding of genetic relatedness of certain species. (12 Dec 1998) |
| N-(5-amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5'-phosphate synthetase | <enzyme> 5-amino-1-ribosyl-4-imidazole carboxylic acid 5'-phosphate (carboxy-air), ATP and aspartate yield n(5-amino-4-imidazolylcarbonyl)-l-aspartic acid 5'-phosphate(succino-aicar), ADP and p Registry number: EC 6.3.4.- (26 Jun 1999) |
| N(6)-(6-carbamoylhexyl)-FAD-D-amino acid oxidase | <enzyme> A semi-synthetic oxidase; prepared by reacting the succinimido ester of n(6)-(6-carboxyhexyl)-fad with apo-d-amino acid oxidase from pig kidney in the presence of the benzoate Registry number: EC 1.4.3.- Synonym: nch-fad-daao (26 Jun 1999) |
| N-carbamoyl-D-amino acid amidohydrolase | <enzyme> From comamonas sp.e222c; mw 120 kD; hydrolyzes d-enantiomers of various n-carbamoyl-d-amino acids to d-amino acids, ammonia and co2; sensitive to thiol reagents; does not require metal ions Registry number: EC 3.5.1.- Synonym: caa-amidohydrolase, carbamoyl d-aa amidohyrolase (26 Jun 1999) |
| nonessential amino acid | <biochemistry> The amino acid's that can be synthesised by an organism and are thus not required in the diet. (05 Mar 2000) |
| nonpolar amino acid | An alpha-amino acid in which the functional group attached to the alpha-carbon (i.e., R in RCH(NH2)COOH) has hydrophobic properties; e.g., valine, leucine, alpha-aminobutyrate. (05 Mar 2000) |
| D-amino acid malonyltransferase | <enzyme> From mung beans Registry number: EC 2.3.1.- Synonym: 1-aminocyclopropanecarboxylate malonyltransferase, d-acc-malonyltransferase, acc n-malonyltransferase (26 Jun 1999) |
| d-amino-acid oxidase | <enzyme> Chemical name: D-Amino-acid:oxygen oxidoreductase (deaminating) Registry number: EC 1.4.3.3 (12 Dec 1998) |
| D-amino acid transaminase | <enzyme> Catalyses the alpha,beta elimination of the (d)-isomer of beta-chloroalanine or other amino acids to yield pyruvate, chloride and ammonia Registry number: EC 2.6.1.- (26 Jun 1999) |
| D-amino acid transferase | <enzyme> Mw 41 kD; catalyses d-amino acid transfer; d-configuration specific; recognises aromatic d-amino acid esters to form oligo d-amino acid esters Registry number: EC 2.3.2.- (26 Jun 1999) |
| dibasic amino acid | An amino acid containing a second basic group (usually an amino group); e.g., lysine, arginine, ornithine. Synonym: dibasic amino acid. (05 Mar 2000) |
| essential amino acid | <biochemistry> Those amino acids that cannot be synthesised by an organism and must therefore be present in the diet. The term is often applied anthropocentrically to those amino acids required by humans (Ileu, Leu, Lys, Met, Phe, Thr, Try, & Val), though rats need two more (Arg & His). (18 Nov 1997) |