Custom MemPro™ N-(deoxy)ribosyltransferase-like Membrane Proteins

Creative Biostructure has developed custom MemPro™ gene-to-structure services for N-(deoxy)ribosyltransferase-like membrane proteins in protein expression, purification, structure determination and functional analysis.

N-(deoxy)ribosyltransferase-like superfamily adopts a Flavodoxin-like fold and includes N-deoxyribosyltransferase family, ADP-ribosyl cyclase-like family as well as hypothetical protein PA1492. The structural and mechanistic similarities between N-deoxyribosyltransferase and ADP-ribosyl cyclase-like family remained unknown for a decade until the unraveling of their structures. As predicted by SCOP (Structural Classification of Proteins), PA1942 has a very similar putative active site and thus a possible deoxyribosyltransferase activity.

N-deoxyribosyltransferases (EC 2.4.2.6), also called trans-N-deoxyribosylases, catalyze the exchange of the bound form of purine or pyrimidine bases of 2’-deoxyribonucleosides with the free form of pyrimidine or purine bases. Deoxyribosyltransferases are classified into two classes depending on their substrate specificities: purine transdeoxyribosylase (type I) and nucleoside 2-deoxyribosyltransferase (type II). These enzymes were initially described in lactobacilli, then found in some species of Streptococcus and protozoans, such as Crithidia luciliae, Trypanosoma brucei, Borrelia burgdorferi. Nowadays, 2’-deoxyribosyltransferases are getting increasingly more attention due to its critical role in the synthesis of natural and non-natural nucleosides. Moreover, since several non-natural nucleosides with the sugar moiety modifications can act as antiviral or anticancer agents, it is interesting to explore the possibility of developing novel and effective industrial biocatalysts for the synthesis of natural and modified nucleosides.

ADP-ribosyl cyclase-like family catalyzes the cyclization of the intermediary metabolite, Nicotinamide Adenine Dinucleotide (NAD+), into the putative second messenger cyclic ADP-ribose (cADPr). ADP-ribosyl cyclase activity is found in bacteria, plants and metazoans, and predicted to control the metabolic pathways and other fundamental cellular processes. Mammals have two ADP-ribosyl cyclases identified as CD38 and CD157, both of which function as ectoenzymes and receptors simultaneously. CD38, a regulator of cell activation and proliferation, is involved in the adhesion process between lymphocytes and endothelial cells in human. CD157 is however prevalently expressed in the cells of myeloid lineage.

Creative Biostructure can provide custom MemPro™ gene-to-structure services for membrane proteins.