Purification and Properties of Acid Carboxypeptidase II from Aspergillus oryzae |
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Authors: | Tadanobu Nakadai Seiichi Nasuno Nobuyoshi Iguchi |
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Affiliation: | Noda Institute for Scientific Research, Noda-shi, Chiba-ken |
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Abstract: | Acid carboxypeptidase II from Aspergillus oryzae was purified from the rivanol non-precipitated fraction. The purified enzyme was homogeneous on polyacrylamide gel disc electrophoresis. The optimum activity of the enzyme lay at pH 3.0 for carbobenzoxy-L-glutamyl-l-tyrosine. The enzyme was inhibited by diisopropylphosphorofluoridate and SH reagents such as p-chloromercuribenzoate and monoiodoacetate, but not by such metal chelating agents as ethylenediaminetetraacetate, α, α′-dipyridyl and o-phenanthroline. The molecular weight of the enzyme was estimated to be about 105,000. |
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Keywords: | cysteine tryptophylquinone cofactor directed mutagenesis fusion reporter method l-lysine ε-oxidase (LodA) LodB |
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