Purification and characterization of the enantioselective nitrile hydratase from Rhodococcus equi A4
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
11330707
DOI
10.1007/s002530000507
Knihovny.cz E-resources
- MeSH
- Hydro-Lyases chemistry isolation & purification metabolism MeSH
- Isoelectric Point MeSH
- Hydrogen-Ion Concentration MeSH
- Methanol pharmacology MeSH
- Molecular Weight MeSH
- Nitriles metabolism MeSH
- Protein Subunits MeSH
- Rhodococcus equi enzymology MeSH
- Solvents pharmacology MeSH
- Amino Acid Sequence MeSH
- Stereoisomerism MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Hydrocarbons pharmacology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Hydro-Lyases MeSH
- Methanol MeSH
- nitrile hydratase MeSH Browser
- Nitriles MeSH
- Protein Subunits MeSH
- Solvents MeSH
- Hydrocarbons MeSH
The nitrile hydratase from Rhodococcus equi A4 consisted of two kinds of subunits which slightly differed in molecular weight (both approximately 25 kDa) and showed a significant similarity in the N-terminal amino acid sequences to those of the nitrile hydratase from Rhodococcus sp. N-774. The enzyme preferentially hydrated the S-isomers of racemic 2-(2-, 4-methoxyphenyl)propionitrile, 2-(4-chlorophenyl)propionitrile and 2-(6-methoxynaphthyl)propionitrile (naproxennitrile) with E-values of 5-15. The enzyme functioned in the presence of 5-98% (v/v) of different hydrocarbons, alcohols or diisopropyl ether. The addition of 5% (v/v) of n-hexane, n-heptane, isooctane, n-hexadecane, pristane and methanol increased the E-value for the enzymatic hydration of 2-(6-methoxynaphthyl)propionitrile.
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