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- W2024972610 abstract "Abstract Free d -alanine was detected in a cell extract of the fruit-body of an edible basidiomycetous mushroom, Lentinus edodes (Shiitake), by means of reverse-phase high performance liquid chromatography. We also found an amino acid racemase activity in L. edodes fruit-body, and purified the enzyme. The enzyme has a molecular weight of approximately 86,000, and consists of two subunits of identical molecular weight (44,000). The optimal pH of the enzyme activity is around pH 9.5 for both d -to- l and l -to- d alanine racemization. The enzyme requires pyridoxal 5′-phosphate as a cofactor. K m and V max values for d -alanine were 37.3 mM and 520 nmol/min/mg, respectively; for l -alanine, they were 9.21 mM and 141 nmol/min/mg, respectively. The equilibrium constant was calculated to be 1.10, which is consistent with the theoretical value for the racemase reaction. The ability of the enzyme to catalyze the racemization of various d -amino acids was investigated. The enzyme catalyzes the racemization of d -serine (relative reaction rate, 144% of rate for d -alanine), d -alanine (100%), d -homoserine (17.1%), d -2-aminobutyrate (5.6%), d -glutamate (4.5%), and d -asparagine (3.2%). To the best of our knowledge, this is the first report of an amino acid racemase produced by a basidiomycetous mushroom." @default.
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- W2024972610 date "2003-09-01" @default.
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- W2024972610 title "Occurrence of a unique amino acid racemase in a basidiomycetous mushroom, Lentinus edodes" @default.
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- W2024972610 doi "https://doi.org/10.1016/s1381-1177(03)00102-4" @default.
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