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Titlebook: Biochemistry of Vitamin B6 and PQQ; G. Marino,G. Sannia,F. Bossa Conference proceedings 1994 Birkhäuser Verlag 1994 Alanin.Aspartat.Glycog

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https://doi.org/10.1007/978-3-8349-9660-2ase is different from those of other aminotransferases so far studied. Based on the structure, and stereospecificity for C-4′ hydrogen transfer, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase probably evolved from the common ancestral protein, which was different from that of other aminotransferases.
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Stereospecificity of aminotransferases for C-4′ hydrogen transfer and enzyme evolutionase is different from those of other aminotransferases so far studied. Based on the structure, and stereospecificity for C-4′ hydrogen transfer, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase probably evolved from the common ancestral protein, which was different from that of other aminotransferases.
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Redesign of aspartate aminotransferase specificity to that of tyrosine aminotransferasensaminase is to exclude nonspecific substrates by keeping the enzyme in an open inactive form. The free energy to close the enzyme into its active conformation derives from association with specific ligands.
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