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Steady-state kinetic properties of 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831: Steroid substrate specificity and nucleotide cofactor dependency
| Content Provider | Semantic Scholar |
|---|---|
| Author | Ueda, Shigeru Oda, Masayuki Imamura, Shigeyuki Ohnishi, Masatake Nakaragi-Cho, Shimogamo |
| Copyright Year | 2004 |
| Abstract | We investigated the steroid substrate specificity of 3α-hydroxysteroid dehydrogenase (3α-HSD) from Pseudomonas sp. B-0831. Similar to 3α-hydroxysteroid dehydrogenase/carbonyl reducetase (3α-HSD/CR) from Comamonas testosteroni, the recombinant 3α-HSD from P. sp. B-0831 catalyzed the oxidation of the antibiotic fusidic acid with the lowest Km value among 3α-hydroxysteroid substrates examined in this study, while the kcat value was 17% of that for one of the other substrates, androsterone. The enzyme showed the utility of cofactor analogues, such as thio-NAD + , 3-acetylpyridine adenine dinucleotide (APAD + ), and nicotinamide hypoxanthine dinucleotide (deamino-NAD + ). Comparing the effects of cofactors, NAD + and thio-NAD + , on the kcat values, NAD + was preferred for cholic acid, while thio-NAD + was preferred for fusidic acid. These results suggest that the enzyme is adaptable to various substrates and cofactors, thus generating the broad substrate specificity with each different reaction mode. |
| Starting Page | 23 |
| Ending Page | 28 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| Volume Number | 4 |
| Alternate Webpage(s) | http://www.jsb.gr.jp/jbm/2004/0401_3.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
