||Hasegawa D, Kito K, Maeda T, Rai V, Cha-Um S, Tanaka Y, Fukaya M, Takabe T
||Two groups of thermophilic amino acid aminotransferases
exhibiting broad substrate specificities for the synthesis
of phenylglycine derivatives
||Thirty two thermophilic amino acid aminotrans-
ferases (AATs) were expressed in Escherichia coli as
soluble and active proteins. Based on their primary
structures, the 32 AATs were divided into four phylogenetic
groups (classes I, II, IV, and V). The substrate specificities of
these AATs were examined, and 12 AATs were found capable
of synthesizing ring-substituted phenylglycine derivatives
such as hydroxyl-, methoxy-, and fluorophenylglycines.
Eleven out of the 12 AATs were enzymes belonging to two
phylogenetic groups namely, one subgroup of the class I
family and the class IV family. AATs in these two groups may
thus be useful for the synthesis of a variety of ring-substituted phenylglycine derivatives.