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- W2035827123 abstract "An enzyme which catalyzes the transamination of L‐aspartate with 2‐oxoglutarate has been purified 400‐fold to electrophoretic homogeneity from the unicellular green alga Chlamydomonas reinhardtii 6145c. An apparent relative molecular mass of 138 000 was estimated by gel filtration. The enzyme is a dimer consisting of two identical subunits of M r 65000 each as deduced from PAGE/SDS studies. A stoichiometry of two molecules pyridoxal 5‐phosphate/enzyme molecule was calculated. The enzyme has an isoelectric point of 8.48 and its absorption spectrum exhibits a maximum at 412 nm which is shifted to 330 nm upon addition of L‐aspartate. L‐Aspartate or pyridoxal 5‐phosphate, but not 2‐oxoglutarate, protected the enzyme from heat inactivation. The purified enzyme was able to transaminate, although to a low extent, L‐phenylalanine and L‐tyrosine with 2‐oxoglutarate, and L‐serine, L‐alanine and L‐glutamine with oxaloacetate. L‐Aspartate aminotransferase exhibited hyperbolic kinetics for 2‐oxoglutarate and oxaloacetate, and nonhyperbolic behaviour for L‐aspartate and L‐glutamate. Apparent K m values were 0.55 mM for 2‐oxoglutarate, 0.044 mM for oxaloacetate, 2.53 mM for L‐aspartate and 3.88 mM for L‐glutamate. Transamination of L‐aspartate in C. reinhardtii is a bisubstrate reaction with a bi‐bi ping‐pong mechanism, and is not inhibited by substrates." @default.
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- W2035827123 date "1990-03-01" @default.
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- W2035827123 title "Purification and properties of L-aspartate aminotransferase of Chlamydomonas reinhardtii" @default.
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- W2035827123 doi "https://doi.org/10.1111/j.1432-1033.1990.tb15432.x" @default.
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