Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage

Cytochrome P450 2A13 is an omitted brother of CYP2A6 that has an important role in the drug metabolism of liver. Due to extrahepatic expression, it has gained less attention than CYP2A6, despite the fact that it plays a significant role in toxicant-induced pulmonary lesions and, therefore, lung cancer. The purpose of this mini-review is to summarize the basic knowledge about this enzyme in relation to the substrates, inhibitors, genetic polymorphisms, and transcriptional regulation that are known so far (September 2021).

Breeding of Buckwheat to Reduce Bitterness and Rutin Hydrolysis

Buckwheat (Fagopyrum esculentum) is recognized as an important traditional crop in some regions, and its taste is an important characteristic. Of the three cultivated buckwheat species, Tartary buckwheat (Fagopyrum tataricum) and perennial buckwheat (Fagopyrum cymosum) have strong bitterness in their seeds, which has prevented the wider use of the seeds of these varieties. In Tartary buckwheat, some studies have focused on the cause of strong bitterness generation. Tartary buckwheat seeds contain large amounts of the functional compounds rutin and rutinosidase, and rutin hydrolysis by rutinosidase has been found to be the trigger of rutin hydrolysis. Therefore, a variety with only a trace of rutinosidase and with reduced bitterness is required. The rutinosidase in Tartary buckwheat seeds consists of two major isozymes with very similar enzymatic characteristics, which can hydrolyze flour rutin within several minutes after the addition of water. Recently, the trace-rutinosidase variety Manten-Kirari in Tartary buckwheat was developed. The trace-rutinosidase characteristics were dominated by a single recessive gene. In ‘Manten-Kirari’ dough and foods, such as breads, confectionaries, and noodles, the rutin residual ratio was higher and bitterness was reduced compared to that of the normal-rutinosidase variety. In this review, we summarize the detailed research on the breeding of buckwheat related to reducing bitterness and rutin hydrolysis.

γ-Glutamyltranspeptidase essential for the metabolism of γ-glutamyl compounds in bacteria and its application

ABSTRACT The enzymatic characteristics of γ-glutamyltranspeptidase were elucidated. The catalytic nucleophile of the enzymatic reaction of Escherichia coli γ-glutamyltranspeptidase was identified as the Oγ of the N-terminal Thr-residue of the small subunit. It was demonstrated that the inactive precursor of γ-glutamyltranspeptidase is processed autocatalytically and intramolecularly into the active heterodimeric mature enzyme via an ester intermediate. The catalytic nucleophile of this processing reaction was identified as the same Oγ atom of the N-terminal Thr-residue of the small subunit. These results were also supported by the three-dimensional structures of the γ-glutamyl enzyme intermediate and of the precursor-mimicked T391A nonprocessable mutant enzyme. Applications of transpeptidation and hydrolysis activities of bacterial γ-glutamyltranspeptidases were developed. Using transpeptidation activity, efficient enzymatic production of useful γ-glutamyl compounds, such as prodrug for Parkinson's disease, theanine and kokumi compound, was enabled. Hydrolysis activity was used as glutaminase and the mutant enzymes gaining glutaryl-7-aminocephalosporanic acid acylase activity were isolated.

A Metastasis Suppressor Pt-Dendrimer Nanozyme for the Alleviation of Glioblastoma

Nanozymes are nanostructure-based materials which mimic the enzymatic characteristics of natural enzyme. Biological applications of nanozymes have been highlighted in basic research, industry, and translational medicine as a new cutting-edge...