| anticodon | <molecular biology> Nucleotide triplet on transfer RNA that is complementary to the codon of the messenger RNA. (13 Nov 1997) |
|---|---|
| adenine deaminase | <enzyme> An enzyme that catalyses the hydrolysis of adenine to ammonia and hypoxanthine. A part of purine degradation. (05 Mar 2000) |
| adenosine deaminase | <enzyme> An enzyme that catalyses the hydrolysis of adenosine to inosine with the elimination of ammonia. Since there are wide tissue and species variations in the enzyme, it has been used as a tool in the study of human and animal genetics and in medical diagnosis. Chemical name: Adenosine aminohydrolase Registry number: EC 3.5.4.4 (12 Dec 1998) |
| adenylic acid deaminase | <enzyme> An enzyme that catalyses the deamination of AMP to imp. Chemical name: AMP aminohydrolase Registry number: EC 3.5.4.6 (12 Dec 1998) |
| AMP deaminase | <enzyme> An enzyme that catalyses the deamination of AMP to imp. Chemical name: AMP aminohydrolase Registry number: EC 3.5.4.6 (12 Dec 1998) |
| blasticidin S deaminase | <enzyme> Catalyses deamination of cytosine moiety of blasticidin s Registry number: EC 3.5.4.23 (26 Jun 1999) |
| guanine deaminase | <enzyme> An enzyme that catalyses the deamination of guanine to form xanthine. Chemical name: Guanine aminohydrolase Registry number: EC 3.5.4.3 (12 Dec 1998) |
| phosphoribosylaminopyrimidine deaminase | <enzyme> Intermediate in riboflavin biosynthesis Chemical name: 2,5-diamino-6-oxy-4-(5'-phosphoribosylamino) pyrimidine deaminase Registry number: EC 3.5.4.- (26 Jun 1999) |
| myoadenylate deaminase | Muscle AMP deaminase. See: AMP deaminase. (05 Mar 2000) |
| cytidine deaminase | <enzyme> An enzyme that catalyses the deamination of cytidine, forming uridine. Chemical name: Cytidine aminohydrolase Registry number: EC 3.5.4.5 (12 Dec 1998) |
| S-adenosylhomocysteine deaminase | <enzyme> From streptomyces flocculus; deaminating enzyme responsible for the conversion of s-adenosylhomocysteine to s-inosylhomocysteine Registry number: EC 3.5.4.- Synonym: adohcy deaminase (26 Jun 1999) |
| histidine deaminase | <enzyme> An enzyme of the lyase class that catalyses the reaction of l-histidine to form urocanate and ammonia. The reaction is the initial step of histidine catabolism. Genetic deficiency of the enzyme, transmitted as an autosomal recessive trait, causes histidinaemia. Chemical name: L-Histidine ammonia-lyase Registry number: EC 4.3.1.3 (12 Dec 1998) |
| pterin deaminase | An aminohydrolase catalyzing hydrolytic deamination of 2-amino-4-hydroxypteridine to form 2,4-dihydroxypteridine and ammonia. (05 Mar 2000) |
| homoserine deaminase | <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. Chemical name: L-Cystathionine cysteine-lyase (deaminating) Registry number: EC 4.4.1.1 (12 Dec 1998) |
| serine deaminase | <enzyme> A pyridoxal-phosphate protein that catalyses the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. Chemical name: L-Threonine hydro-lyase (deaminating) Registry number: EC 4.2.1.16 (12 Dec 1998) |