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Glyoxalase pathway, comprising glyoxalase I (GLY I) and glyoxalase II (GLY II) enzymes, is the major pathway for detoxification of methylglyoxal (MG) into D-lactate involving reduced glutathione (GSH).However, in bacteria, glyoxalase III (GLY III) with DJ-1/Pfp I domain(s) can do the same conversion in a single step without GSH.The sequences of DJ-1 proteins were searched against the swiss-prot database using functional Arabidopsis GLY III, At DJ-1d (AT3g02720).

A total of eleven DJ-1 proteins were found to be present in other plant species apart from monocots and dicots such as Bryophyta (Physcomitrella patens), Gymnosperm (Picea sitchensis) and Lycopod (Selaginella moellendorffii).

Among them, Selaginella moellendorffii has five, Picea sitchensis has four and Physcomitrella patens has two DJ-1/Pfp I domain containing proteins (Table 1).

GLY I converts a highly cytotoxic metabolite methylglyoxal (MG) into S-lactoylglutathione (SLG) with the help of reduced glutathione (GSH).

The SLG is further hydrolyzed into D-lactate by GLY II and GSH is recycled back into the system (Fig. Higher concentrations of SLG can inhibit DNA synthesis, hence is considered toxic to the living system Conventional glyoxalase pathway consists of two enzymes (GLY I and GLY II) that detoxify MG into D-lactate with the help of reduced glutathione.

In the present study, we have performed analysis of DJ-1/Pfp I domain containing proteins across plant kingdom in order to explore the existence of this unique alternate and short route of the detoxification of deleterious metabolite-MG.

In order to gain insights into the functional relevance of DJ-1 proteins in rice, we have analyzed expression profiling of these genes at different developmental stages, various tissues and multiple stress conditions.

A total of 217 sequences from various plant taxa were used to perform sequence and phylogenetic analysis.

Given below is the brief description of DJ-1/Pfp I domain containing proteins in monocots, dicots and other species.

Moreover, presence of functional GLY III activity for one of the Os DJ-1 proteins, Os DJ-1C, has been confirmed by enzyme kinetics and site-directed mutagenesis.

It has been shown that Os DJ-1C could convert MG into D-lactate in a single step driven glutathione-independent reaction.

The investigations performed on the DJ-1 members will assist in elaborating the understanding about the evolution of this unique glyoxalase pathway.

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