|
Vladimir
I. Tishkov1, Michail D. Shelomov2, Anastaiya A. Pometun3, Svyatoslav S. Savin4, Denis L. Atroshenko5
Physiological role of D-amino acids and bioanalytical
potential of D-amino acid oxidases
Abstract
Abstract. D-amino acid oxidase (DAAO) plays an important role in the
functioning of both prokaryotes and eukaryotes. DAAO is increasingly being used
in practice, including for the determination of D-amino acids in complex
samples, including human tissues and fluids. There are generally two types of
DAAO in all organisms. The first type is an enzyme highly specific for
D-aspartate and has its own name D-aspartate oxidase (DASPO). DAAO of the
second type is characterized by a wide spectrum of substrate specificity, with
preference for one or another D-amino acid varying from source to source. The
activity of DAAO with a large number of substrates greatly complicates the
selective determination of a particular D-amino acid. The problem is often
solved by choosing an enzyme that, under the conditions of analysis, has low or
no activity with other D-amino acids present in the sample. For the convenience
of selecting a particular enzyme, we have collected and analyzed literature
data on the catalytic parameters of known DAAOs with the most important D-amino
acids. In addition, similar data are presented for novel recombinant DAAOs from
the methylotrophic yeast Ogataea parapolymorpha DL-1. Analysis of the
data shows that, with the D-amino acid series, the new OpaDASPO and OpaDAAO
have the highest catalytic parameters.
Key words: D-amino
acid oxidase, physiological role, catalytic parameters, substrate specificity, Ogataea
parapolymorpha DL-1
Copyright (C) Chemistry Dept., Moscow State University, 2002
|
|
