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Spider’s venom phospholipases D: A structural review
- Masood, Rehana, Ullah, Kifayat, Ali, Hamid, Ali, Ijaz, Betzel, Christian, Ullah, Anwar
- International journal of biological macromolecules 2017
- Araneae, catalytic activity, crystal structure, databases, peptides, phospholipases, proteins, spider venoms, triose-phosphate isomerase
- Spider venoms are complex mixtures of proteins, peptides and small organic and inorganic molecules. Among the proteins, phospholipases D (PLDs) present the major portion, and till now they are the most studied enzymes in spider venom. These PLDs have been divided into two classes, I and II, based on their primary and tertiary structure. Currently, crystal structures of both classes of these enzymes are available in the Protein Data Bank (PDB). Their three-dimensional structure is composed of eight α-helices and eight β-strands forming the ubiquitous fold called triosephosphate isomerase (TIM) barrel. These enzymes use general acid-base catalysis to hydrolyzes their substrate. In this review, we have described the structural features, structure-based mechanisms of catalysis, maturation, and inhibition of these enzymes using the synthetic inhibitor.