S-adenosylmethionine decarboxylase from baker's yeast
| Autor: | Juhani Jänne, R Sinervirta, H Pösö |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Adenosylmethionine Decarboxylase
Benzylamines Mitoguazone Stereochemistry Carboxy-Lyases Spermidine Borohydrides Saccharomyces cerevisiae Diamines Biochemistry Spermidine Synthase Chromatography Affinity chemistry.chemical_compound Isoniazid Putrescine Pyridoxal phosphate Molecular Biology Cadaverine Cyanides biology Sepharose Methylglyoxal Cell Biology Semicarbazides Spermidine synthase activity chemistry Adenosylmethionine decarboxylase Pyridoxal Phosphate biology.protein Spermidine synthase Research Article |
| Zdroj: | The Biochemical journal. 151(1) |
| ISSN: | 0264-6021 |
| Popis: | 1. S-Adenosyl-L-methionine decarboxylase (S-adenosyl-L-methionine carboxy-lyase, EC 4.1.1.50) was purified more than 1100-fold from extracts of Saccharomyces cerevisiae by affinity chromatography on columns of Sepharose containing covalently bound methylglyoxal bis(guanylhydrazone) (1,1′[(methylethanediylidene)dinitrilo]diguanidine) [Pegg, (1974) Biochem J. 141, 581-583]. The final preparation appeared to be homogeneous on polyacrylamide-gel electrophoresis at pH 8.4. 2. S-Adenosylmethionine decarboxylase activity was completely separated from spermidine synthase activity [5′-deoxyadenosyl-(5′),3-aminopropyl-(1),methylsulphonium-salt-putrescine 3-aminopropyltransferase, EC 2.5.1.16] during the purification procedure. 3. Adenosylmethionine decarboxylase activity from crude extracts of baker's yeast was stimulated by putrescine, 1,3-diamino-propane, cadaverine (1,5-diaminopentane) and spermidine; however, the purified enzyme, although still stimulated by the diamines, was completely insensitive to spermidine. 4. Adenosylmethionine decarboxylase has an apparent Km value of 0.09 mM for adenosylmethionine in the presence of saturating concentrations of putrescine. The omission of putrescine resulted in a five-fold increase in the apparent Km value for adenosylmethionine. 5. The apparent Ka value for putrescine, as the activator of the reaction, was 0.012 mM. 6. Methylglyoxal bis(guanylhydrazone) and S-methyladenosylhomocysteamine (decarboxylated adenosylmethionine) were powerful inhibitors of the enzyme. 7. Adenosylmethionine decarboxylase from baker's yeast was inhibited by a number of conventional carbonyl reagents, but in no case could the inhibition be reversed with exogenous pyridoxal 5′-phosphate. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|