Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+1-glutamate.
A previously unrecognized enzyme, citrate lyase deacetylase, has been purified about 140-fold from cell extracts of Rhodopseudomonas gelatinosa. It catalyzed the conversion of enzymatically active acetyl-S-citrate lyase into the inactive HS-form and acetate. The enzyme exhibited an optimal rate of i...
Uloženo v:
| Vydáno v: | J Bacteriol |
|---|---|
| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1975
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC236005/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/356/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.124.3.1052-1061.1975 |
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