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Specific in vivo cleavage of D-serine deaminase and properties of tetrameric polypeptide aggregates of the fragments.
The primary D-serine deaminase (D-serine dehydratase, EC 4.2.1.14) of Escherichia coli K-12 is unstable within the cell. The protein, a single polypeptide chain, is cleaved at a lysine residue by a cellular proteolytic activity. Fragments containing the active site then aggregate into tetramers, whi...
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| Autori principali: | , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
1976
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC233267/ https://ncbi.nlm.nih.gov/pubmed/770418 |
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