Affiliation:
1. Lomonosov Moscow State University; Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences, Moscow, Russian Federation
2. Lomonosov Moscow State University, Moscow, Russian Federation
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 fl uids. There are generally two types of DAAO in all organisms. The fi rst type is
an enzyme highly specifi c 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.
Funder
Russian Foundation for Basic Research
Cited by
1 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献