Purification and Characterization of N-Acetylglucosamine-6-phosphate Deacetylase from a Psychrotrophic Marine Bacterium, Alteromonas Species
| Autor: | Chieko Endo, Shizu Fujishima, Nami Sakata, Noriko Higashida, Akihiko Maruyama, Naoko Yamano, Takanori Higashihara |
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| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Molecular mass Biology medicine.disease_cause biology.organism_classification Applied Microbiology and Biotechnology Microbiology carbohydrates (lipids) Enzyme chemistry Biochemistry Vibrio cholerae medicine Enzyme kinetics Thermolabile Alteromonas Psychrophile Bacteria |
| Zdroj: | Marine Biotechnology. 2:57-64 |
| ISSN: | 1436-2228 |
| DOI: | 10.1007/s101269900008 |
| Popis: | A psychrotrophic bacterium, strain Mct-9, which produced an N-acetylglucosamine-6-phosphate deacetylase, was isolated from a deep-seawater sample in the Mariana Trough. The Mct-9 strain was identified as Alteromonas sp. The native enzyme had a molecular mass of 164,000 Da, and was predicted to be composed of four identical subunits with molecular masses of 41,000 Da. The purified enzyme hydrolyzed N-acetylglucosamine (GlcNAc), GlcNAc-6-phosphate, and GlcNAc-6-sulfate. Considering the low K(m) and high k(cat)/K(m) for GlcNAc-6-phosphate, it probably acts as a GlcNAc-6-phosphate deacetylase in vivo. The enzyme was functional in the temperature range of 5 degrees to 70 degrees C and displayed optimal activity at 55 degrees C. The optimal temperature was higher than that of the deacetylase from the mesophilic bacterium Vibrio cholerae non-O1. The characteristics of the GlcNAc-6-phosphate deacetylase from Alteromonas sp. are unique among psychrotrophs and psychrophiles, whose intracellular enzymes are mostly thermolabile. |
| Databáze: | OpenAIRE |
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