ABSTRACT
This chapter describes an example of enzyme research. In the previous chapters, examples are shown for the better understanding of the respective topics. The enzyme, l-phenylalanine oxidase (deaminating and decarboxylating) (PAO), is unique in that it catalyzes both oxidative deamination and oxygenative decarboxylation of l-Phe, l-Tyr, and l-Met, and highly specific to l-Phe. Moreover, the structural studies of PAO revealed a novel type of activation, that is, PAO is expressed as pro-enzyme (proPAO), and the removal of the prosequence which occupies the substrate channel results in the activation of enzyme. 10.1 Introduction
l-Phe oxidase (deaminating and decarboxylating) was purified from Pseudomonas sp. P-501 by H. Koyama of Noda Institute for Scientific Research (Japan) in 1983 [1]. Dr. Koyama and we started to collaborate on the kinetic study of the enzyme. We have studied on the enzyme kinetically and structurally since then. So it is worth to look back at the works here.
