Summary
The nucleotide sequence of the E.coli ilvE gene, which encodes branched-chain amino acid aminotranferase (IlvAT), was determined. The enzyme was overproduced by inserting the ilvE gene into a vector with a tac promotor.
The primary, secondary, and quaternary structures of IlvAT were different from those of aspartate aminotransferase (AspAT). The absorption spectrum of the holoenzyme showed no detectable pH-dependent change in the range of pH 5 to 9. Besides branched-chain amino acids, Met, Phe, Tyr, and Trp served as amino donor to 2-oxoglutarate with a lower extent.
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© 1987 Birkhäuser Verlag Basel
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Kuramitsu, S., Inoue, K., Kagamiyama, H. (1987). Branched-Chain Amino Acid Aminotransferase from Escherichia Coli. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_27
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_27
Publisher Name: Birkhäuser, Basel
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