| mAD, MADA | muscle adenylate deaminase; myoadenylate deaminase |
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| ADA | adenosine deaminase; American Dental Association; American Dermatological Association; American Diab... |
| ADase | adenosine deaminase |
| ADCP | adenosine deaminase complexing protein |
| ADD | acceptable daily dose; adduction; adenosine deaminase; attentional deficit disorder; average daily d... |
| ADA | Adenosin deaminase |
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| ADA | Adenosine Deaminase activity |
| CD | Cytidine Deaminase |
| CDA | Cytidine deaminase |
| CDD | Cytidine deaminase |
| deaminase | <enzyme> An enzyme which removes amino groups from compounds, producing ammonia in the process. (09 Oct 1997) |
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| deaminases | Enzymes catalyzing simple hydrolysis of C-NH2 bonds of purines, pyrimidines, and pterins, usually named in terms of the substrate, e.g., guanine deaminases, adenosine deaminases, AMP deaminases, pterin deaminases and thus producing ammonia; not generally used for deamination of noncyclic amides. Deaminases are distinguished from ammonia-lyases (EC group 4.3.1) in that the latter produce an unsaturation at the point of NH3 removal. Synonym: deaminating enzymes. (05 Mar 2000) |
| adenine deaminase | <enzyme> An enzyme that catalyses the hydrolysis of adenine to ammonia and hypoxanthine. A part of purine degradation. (05 Mar 2000) |
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| 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) |
| 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 |
a term used in the trivial names of some aminohydrolases (q.v.), usually restricted to those deaminating cyclic amidines; the enzymes are generally named for their substrates (e.g., adenosine deaminase).
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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