In Search of Engineered Prokaryotic Chlorophyllases: A Bioinformatics Approach
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Chlorophyllase (Chlase) is considered as the first and most important enzyme in chlorophyll degradation pathway. Although there is abundant information regarding plant Chlases and their biological functions, comparatively little is known about their prokaryotic counterparts. In the present study, we employed several bioinformatics tools to assess the phylogenetic relationships in bacterial and cyanobacterial Chlases as well as predicting their molecular and physicochemical properties. The phylogenetic tree analysis classified the bacterial and cyanobacterial chlorophyllases into three distinct clades. All bacterial and cyanobacterial chlorophyllases possessed at least one alpha/ beta hydrolase family domain (pfam12695). Cyanobacterial chlorophyllases pI analysis indicated that they generally have acidic pH, while the pI of bacterial chlorophyllases ranged from acidic (4.58) to highly basic (10.78). Cyanobacterial chlorophyllases generally contained 1 disulfide bond, while bacterial chlorophyllases averagely contained 3 disulfide bonds. Interestingly, while cyanobacterial chlorophyllases contained one or two N-glycosylation sites, bacterial chlorophyllases contained higher numbers of N-glycosylation sites (6 and 7). The findings of the present study would be useful in paving the road for sophisticated engineering of prokaryotic chlorophyllases for biotechnological applications. It was also exhibited that catalytic triad (serine, glutamate or aspartate and histidine) is a critical factor for chlorophyllase activity.
Keywordschlorophyllase bioinformatics physicochemical properties catalytic domains enzyme solubility
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