Subtilisin

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Revision as of 13:11, 15 September 2019

Subtilisin (deepskyblue) complex with streptomycin inhibitor (green) and Ca+2 ions (green) (PDB entry 2sic)

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Updated on 15-September-2019

↑ 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

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 == Structural highlights ==
-The active site of Sub contains the <scene name='43/430882/Cv/4'>catalytic triad: Ser-His-Asp</scene>. The <scene name='43/430882/Cv/8'>peptide inhibitor has numerous interactions with Sub</scene> and the <scene name='43/430882/Cv/11'>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>