Structure of the Hydrolyzed Product (F-2) Released from γ-Polyglutamic Acid by γ-Glutamyl Hydrolase YwtD ofBacillus subtilis
| Autor: | Orawan Chunhachart, Yasutaka Tahara, Momoe Hidesaki, Tatsuhiro Hanayama, Hiroyuki Tanimoto |
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| Rok vydání: | 2006 |
| Předmět: |
chemistry.chemical_classification
biology Molecular mass Chemistry Organic Chemistry Polyglutamic acid gamma-Glutamyl Hydrolase General Medicine Bacillus subtilis biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Molecular Weight Hydrolysis chemistry.chemical_compound γ glutamyl hydrolase Enzyme Polyglutamic Acid Hydrolase Chromatography Gel Molecular Biology Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 70:2289-2291 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.60108 |
| Popis: | The structure of the hydrolyzed product (F-2) with a molecular mass of about 2 kDa released from gamma-polyglutamic acid by the gamma-glutamyl hydrolase YwtD of Bacillus subtilis was analyzed. The results showed that F-2 is an optically heterogeneous polymer consisting of D- and L-glutamic acid in an 80:20 ratio with D-glutamic acid on both the N- and C-terminal sides, suggesting that YwtD is an enzyme that cleaves the gamma-glutamyl bond between D- and D-glutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region. |
| Databáze: | OpenAIRE |
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