Subtilisin: Difference between revisions

Revision as of 16:11, 15 September 2019

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^[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].

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

Drag the structure with the mouse to rotate

3D Structures of Subtilisin3D Structures of Subtilisin

Updated on 15-September-2019

Native mature subtilisin
- 2z2x – TkSub - Thermococcus kodakarensis
- 1sca, 1scb, 1sbc, 3unx – BsSub - Bacillus subtilis (Subtilisin Carlsberg)
- 1pxq – BsSub - NMR
- 1gns, 1sup, 1st2, 1s01, 1sbt, 2sbt, 2st1 – BaSub - Bacillus amyloliquefaciens
- 1ea7, 3d43, 2ixt – spehricase – Sub from Bacillus sphaericus
- 2gko, 3vyv, 4dww – BsSub – Bacillus subtilis
Mutant mature subtilisin
- 3f49, 3co0, 2zrq, 3vhq – TkSub (mutant)
- 1gnv, 1dui, 1sue, 1a2q, 1aqn, 1sua, 1au9, 1ak9, 1yja, 1yjb, 1yjc, 1sbh, 1sbi, 1sub, 1suc, 1sud, 1s02 – BaSub (mutant)
- 2xrm - BcSub residues 19-321 - Bacillus clausii
Unautoprocessed subtilisin (pro-Sub)
- 2z2z, 2e1p – pro-TkSub
- 2zwo, 2zwp, 4jp8, 3wiu, 3wiv – pro-TKSub (mutant)
- 2wv7 – pro-BcSub
- 2wwt, 2x8j - pro-BcSub (mutant)
- 3whi - pro-BcSub (mutant)
Mature subtilisin complexed with its propeptide
- 3cnq – BaSub
- 1spb – BaSub (mutant)
- 3a3n, 3a3o, 3a3p, 2z56, 2z57, 2z58, 2z2y, 2z30 – TkSub
- 3vv2 – TkSub (mutant)
- 1scj – BsSub
Subtilisin complexed with polypeptide inhibitor
- 1y1k, 1y33, 1y34, 1y3b, 1y3c, 1y3d, 1y3f, 1y48, 1y4a, 1y4d, 1tm3, 1tm4,
- 1tm1, 1lw6 – BaSub+ chymotripsin inhibitor 2
- 1tm5, 1tm7, 1tmg, 1to1, 1to2 - BaSub+ chymotrypsin inhibitor 2 (mutant)
- 3sic, 5sic, 2sic – BaSub+Streptomyces inhibitor SSI
- 1yu6 – BsSub+ovomucoid
- 1v5i – BaSubb+POIA1 peptide
- 1r0r – BsSub+ovomucoid
- 1oyv – BsSub+tomato inhibitor II
- 1sbn, 1sib, 2sec, 1cse – BsSub+Elgin C
- 2sni - BaSub+Elgin C2
- 1mee - BpSub+Elgin C – Bacillus pumilus
Subtilisin complexed with inhibitor
- 3bgo – BaSub+azide
- 1c3l – BsSub+Xe
- 1be8 – BsSub+cinnamoyl
- 1be6 - BsSub+cinnamoyl+acetonitrile
- 1bfk, 1scd – BsSub+acetonitrile
- 1bfu, 1af4 – BsSub+dioxane
- 1av7, 1avt, 3vsb, 1vsb – BsSub+boronic acid derivatives
- 1scn – BsSub+carbamate derivative
- 1bh6 – BliSub DY+benzyloxycarbonyl-ala-pro-phe-chloromethyl ketone – Bacillus licheniformis
- 2wuv, 2wuw – BliSub fragment+acetonitrile
- 4c3u – BliSub + Ca + Cs
- 4c3v – BliSub + Ca
Selenosubtilisin
- 1ubn – BaSel-Sub
- 1sel – BsSel-Sub
Savinase
- 3bx1, 1svn, 4cfy, 4cfz, 4cg0, 1iav, 1gci, 1jea, 1st3, 5aqe, 5arb, 5arc, 5ard – BlSav – Bacillus lentus
- 1ndu, 1q5p, 1c9j, 1c9m, 1c9n – BlSav (mutant)
- 1tk2, 1ndq – BlSav+gramicidin S
- 4hx2 – BlSav + Ca + Zn + sermetstatin

ReferencesReferences

↑ 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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Alexander Berchansky, Michal Harel, Joel L. Sussman

[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

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@@ Line 10: / Line 10: @@
 == 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>