Properties of oxaloacetate decarboxylase from Veillonella parvula.
Oxaloacetate decarboxylase was purified to 136-fold from the oral anaerobe Veillonella parvula. The purified enzyme was substantially free of contaminating enzymes or proteins. Maximum activity of the enzyme was exhibited at pH 7.0 for both carboxylation and decarboxylation. At this pH, the Km value...
Uloženo v:
| Vydáno v: | J Bacteriol |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1982
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC216347/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7076619/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.150.3.1252-1258.1982 |
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