Subtilisin
From Proteopedia
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<StructureSection load='' size='350' side='right' caption='Subtilisin (deepskyblue) complex with streptomycin inhibitor (green) and Ca+2 ions (green) (PDB entry [[2sic]])' scene='43/430882/Cv/2'> | <StructureSection load='' size='350' side='right' caption='Subtilisin (deepskyblue) complex with streptomycin inhibitor (green) and Ca+2 ions (green) (PDB entry [[2sic]])' scene='43/430882/Cv/2'> | ||
== Function == | == Function == | ||
- | [[Subtilisin]] is a serine protease. A | + | [[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<ref>PMID:4967581</ref>. See detalis in [[User:Tommie Hata/Introduction to Protein Engineering-Subtilisin]]. |
*'''Selenosubtilisin''' is a semisynthetic selenoenzyme produced by chemical modification of subtilisin<ref>PMID:8385489</ref>.<br /> | *'''Selenosubtilisin''' is a semisynthetic selenoenzyme produced by chemical modification of subtilisin<ref>PMID:8385489</ref>.<br /> | ||
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== Structural highlights == | == Structural highlights == | ||
The active site of Sub contains the <scene name='43/430882/Cv/12'>catalytic triad: Ser-His-Asp</scene>. The <scene name='43/430882/Cv/13'>peptide inhibitor has numerous interactions with Sub</scene> and the <scene name='43/430882/Cv/14'>scissile bond is flanked by Cys-Pro-Met-Val</scene><ref>PMID:1920411</ref>. | The active site of Sub contains the <scene name='43/430882/Cv/12'>catalytic triad: Ser-His-Asp</scene>. The <scene name='43/430882/Cv/13'>peptide inhibitor has numerous interactions with Sub</scene> and the <scene name='43/430882/Cv/14'>scissile bond is flanked by Cys-Pro-Met-Val</scene><ref>PMID:1920411</ref>. | ||
- | </StructureSection> | ||
== 3D Structures of Subtilisin == | == 3D Structures of Subtilisin == | ||
+ | [[Subtilisin 3D structures]] | ||
- | + | </StructureSection> | |
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- | **[[3bx1]], [[1svn]], [[4cfy]], [[4cfz]], [[4cg0]], [[1iav]], [[1gci]], [[1jea]], [[1st3]], [[5aqe]], [[5arb]], [[5arc]], [[5ard]] – BlSav – ''Bacillus lentus''<br /> | ||
- | **[[1ndu]], [[1q5p]], [[1c9j]], [[1c9m]], [[1c9n]] – BlSav (mutant)<br /> | ||
- | **[[1tk2]], [[1ndq]] – BlSav+gramicidin S <br /> | ||
- | **[[4hx2]] – BlSav + Ca + Zn + sermetstatin<br /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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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
- ↑ 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