| PBGD | porphobilinogen deaminase |
|---|---|
| mAD, MADA | muscle adenylate deaminase; myoadenylate deaminase |
| PBG | porphobilinogen |
| PBGS, PBG-S | porphobilinogen synthase |
| PGB | porphobilinogen; prostaglandin B |
| PBGD | Porphobilinogen Deaminase |
|---|---|
| PBG | Porphobilinogen |
| PBGS | Porphobilinogen synthase |
| ADA | Adenosin deaminase |
| ADA | Adenosine Deaminase activity |
| porphobilinogen | <chemical> Chemical name: 1H-Pyrrole-3-propanoic acid, 5-(aminomethyl)-4-(carboxymethyl)- (12 Dec 1998) |
|---|---|
| porphobilinogen oxygenase | <enzyme> Porphobilinogen is converted to 5-oxo-porphobilinogen Registry number: EC 1.13.- (26 Jun 1999) |
| porphobilinogen synthase | <enzyme> An enzyme that catalyses the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. Chemical name: 5-Aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing) Registry number: EC 4.2.1.24 (12 Dec 1998) |
| porphobilinogen synthase porphyria | An inherited disorder in which there is a deficiency of porphobilinogen synthase; d-aminolevulinate levels are elevated, leading to neurological disturbances. Synonym: porphobilinogen synthase porphyria. (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) |
| 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) |
| porphobilinogen deaminase |
hydroxymethylbilane synthase.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
|
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|