Subtilisin
From Proteopedia
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| + | <StructureSection load='2sic' size='350' side='right' caption='Subtilisin (magenta) complex with streptomycin inhibitor (wheat) (PDB entry [[2sic]])' scene=''> | ||
== Function == | == Function == | ||
[[Subtilisin]] is a serine protease. A 77 amino acid propeptide is cleaved from the N-terminus of pro-Sub to create the mature active enzym<ref>PMID:4967581</ref>. See detalis in [[User:Tommie Hata/Introduction to Protein Engineering-Subtilisin]]. | [[Subtilisin]] is a serine protease. A 77 amino acid propeptide is cleaved from the N-terminus of pro-Sub to create the mature active enzym<ref>PMID:4967581</ref>. See detalis in [[User:Tommie Hata/Introduction to Protein Engineering-Subtilisin]]. | ||
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== Relevance == | == Relevance == | ||
Subtilisin is widely used commercially in detergents. | Subtilisin is widely used commercially in detergents. | ||
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| + | == Structural highlights == | ||
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| + | </StructureSection> | ||
== 3D Structures of Subtilisin == | == 3D Structures of Subtilisin == | ||
Revision as of 08:14, 4 September 2016
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3D Structures of Subtilisin
Updated on 04-September-2016
References
- ↑ 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
- ↑ 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
- ↑ 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
