Subtilisin

From Proteopedia

spinqualitylabelsall models Subtilisin (deepskyblue) complex with streptomycin inhibitor (green) and Ca+2 ions (green) (PDB entry 2sic) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D Structures of Subtilisin Function Subtilisin is a serine protease. A 106 amino acid propeptide is cleaved from the N-terminus of pro-subtilisin to create the mature active enzym[1]. See detalis in User:Tommie Hata/Introduction to Protein Engineering-Subtilisin. Selenosubtilisin is a semisynthetic selenoenzyme produced by chemical modification of subtilisin[2]. Savinase is a subtilisin produced from a lentil[3]. Relevance Subtilisin is widely used commercially in detergents. Structural highlights The active site of Sub contains the . The and the [4]. 3D Structures of Subtilisin Subtilisin 3D structures

References

1. ↑ Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. PMID:4967581
2. ↑ Bell IM, Fisher ML, Wu ZP, Hilvert D. Kinetic studies on the peroxidase activity of selenosubtilisin. Biochemistry. 1993 Apr 13;32(14):3754-62. PMID:8385489
3. ↑ Garcia-Mora P, Penas E, Frias J, Martinez-Villaluenga C. Savinase, the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties. J Agric Food Chem. 2014 May 7;62(18):4166-74. doi: 10.1021/jf500849u. Epub 2014, Apr 28. PMID:24738747 doi:http://dx.doi.org/10.1021/jf500849u
4. ↑ Takeuchi Y, Satow Y, Nakamura KT, Mitsui Y. Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J Mol Biol. 1991 Sep 5;221(1):309-25. PMID:1920411