Coding

Part:BBa_K4496000

Designed by: Ana Paula Contelli Xavier, Larissa de Souza Kawanisi   Group: iGEM22_USP-EEL-Brazil   (2022-09-14)

This part is the Jararhagin gene optimized for Pichia pastoris yeast, a highly hemorrhagic P-III SVMP (metalloprotease) class protein from Bothrops Jararaca venom. It has a molecular mass of 52 kDa, which is considered high. In the catalytic domain is the zinc-binding sequence HEXXHXXGXXH and the Met-turn structure, which helps stabilize the three histidine residues involved in catalysis (Bode et al., 1993; Stöcker et al., 1995). In the disintegration domain, there is conservation of the cysteine residues in the same position as those found in RGD, but with replacement by an ECD sequence, common to other P-III SVMPS. That is, it has the disintegration domain (BJARNASON; FOX, 1995). The cysteine-rich disintegrin domains have high similarities to domains found in ADAMs (Paine et. al., 1992).

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