| MAD | major affective disorder; mandibulo-acral dysplasia; maximum allowable dose; methylandrostenediol; m... |
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| PBGD | porphobilinogen deaminase |
| AHH | alpha-hydrazine analog of histidine; anosmia and hypogonadotropic hypogonadism [syndrome]; arylhydro... |
| FHIT | fragile histidine triad [gene] |
| HDC | histidine decarboxylase; human diploid cell; hypodermoclysis |
| 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) |
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| 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) |
| 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) |
| dcmp deaminase | <enzyme> An enzyme that catalyses the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. Chemical name: dCMP aminohydrolase Registry number: EC 3.5.4.12 (12 Dec 1998) |
| deaminase | <enzyme> An enzyme which removes amino groups from compounds, producing ammonia in the process. (09 Oct 1997) |
| dsRNA adenosine deaminase | <enzyme> Catalyses the hydrolytic deamination of adenosine to form inosines; activity simulates double-stranded RNA unwinding; double-stranded RNA is preferred substrate Registry number: EC 3.5.4.- Synonym: double-stranded RNA-specific adenosine deaminase, dsrna-specific adenosine deaminase, red1 (enzyme), red2 (enzyme), adarb2 (26 Jun 1999) |
| threonine 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) |
| 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate deaminase | <enzyme> Forms 5-amino-6-ribitylamino-2,4-(1h,3h)-pyrimidinedione 5'-phosphate, intermediate in biosynthesis of riboflavin Registry number: EC 3.5.4.- Synonym: drap 5'-p deaminase (26 Jun 1999) |
| 3-aminobutyryl-CoA deaminase | <enzyme> Forms crotonyl CoA Registry number: EC 4.3.1.- Synonym: 3-aminobutyryl-coenzyme a deaminase (26 Jun 1999) |
| folic acid deaminase | <enzyme> Chemotaxis regulating enzyme; splits folic acid into 6-hydroxymethylpterin and p-aminobenzoylglutamic acid Registry number: EC 3.5.4.- Synonym: folic acid inactivating enzyme, folic acid c9-n10 cleaving enzyme (26 Jun 1999) |