Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides.

An enantioselective amidase from Rhodococcus erythropolis MP50 was purified to homogeneity. The enzyme has a molecular weight of about 480,000 and is composed of identical subunits with molecular weights of about 61,000. The NH2-terminal amino acid sequence was significantly different from previousl...

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Vydáno v:	J Bacteriol
Hlavní autoři:	Hirrlinger, B, Stolz, A, Knackmuss, H J
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1996
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC178119/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8655547/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.178.12.3501-3507.1996
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