Enzyme-bound pyridoxamine phosphate intermediate

In nature, aminotransferases participate in a number of metabolic pathways [4[. They catalyze the transfer of an amino group originating from an amino acid donor to a 2-ketoacid acceptor by a simple mechanism. First, an amino group from the donor is transferred to the cofactor pyridoxal phosphate with formation of a 2-keto add and an enzyme-bound pyridoxamine phosphate intermediate. Second, this intermediate transfers the amino group to the 2-keto add acceptor. The readion is reversible, shows ping-pong kinetics, and has been used industrially in the production ofamino acids [69]. It can be driven in one direction by the appropriate choice of conditions (e.g. substrate concentration). Some of the aminotransferases accept simple amines instead of amino acids as amine donors, and highly enantioselective cases have been reported [70]. 

The binding of a symmetric chromophore to a protein or nucleic acid often induces CD in that chromophore. For example, the bands of enzyme-bound pyridoxal and pyridoxamine phosphates shown in Fig. 14-9 are positively dichroic in CD, but the band of the quinonoid intermediate at 20,400 cm-1 (490 nm) displays negative CD. When "transimination" occurs to form a substrate Schiff base (Eq. 14-26), the CD is greatly diminished. While the coenzyme ring is known to change its orientation (Eq. 14-39 Fig. 14-10), it is not obvious how the change in environment is related to the change in CD. 

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