Subtilisin: Difference between revisions

Revision as of 11:50, 4 September 2016

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 catalytic triad: Ser-His-Asp. The peptide inhibitor has numerous interactions with Sub and the scissile bond is flanked by Cys-Pro-Met-Val^[4].

Subtilisin (magenta) complex with streptomycin inhibitor (wheat) 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 04-September-2016

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, 1sni, 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 – 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

[1]

[2]

[3]

[4]

@@ Line 24: / Line 24: @@
 **[[1pxq]] – BsSub - NMR<br />
 **[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub  - ''Bacillus amyloliquefaciens''<br />
-**[[1iav]], [[1gci]], [[1jea]], [[1st3]] – BlSub - ''Bacillus lentus'' (Subtilisin Savinase)<br />
 **[[1ea7]], [[3d43]], [[2ixt]] – spehricase – Sub from ''Bacillus  sphaericus''<br />
 **[[2gko]], [[3vyv]], [[4dww]] – BsSub – ''Bacillus subtilis''
@@ Line 32: / Line 31: @@
 **[[3f49]], [[3co0]], [[2zrq]], [[3vhq]] – TkSub (mutant) <br />
 **[[1gnv]], [[1dui]], [[1sue]], [[1a2q]], [[1aqn]], [[1sua]], [[1au9]], [[1ak9]], [[1yja]], [[1yjb]], [[1yjc]], [[1sbh]], [[1sbi]], [[1sub]], [[1suc]], [[1sud]], [[1s02]] – BaSub (mutant)<br />
-**[[1ndu]], [[1q5p]], [[1c9j]], [[1c9m]], [[1c9n]] – BlSub (mutant)<br />
 **[[2xrm]] - BcSub residues 19-321 - ''Bacillus clausii''<br />
@@ Line 59: / Line 57: @@
 **[[1yu6]] – BsSub+ovomucoid <br />
 **[[1v5i]] – BaSubb+POIA1 peptide <br />
-**[[1tk2]], [[1ndq]] – BlSub+gramicidin S <br />
-**[[4hx2]] – BlSub + Ca + Zn + sermetstatin<br />
 **[[1r0r]] – BsSub+ovomucoid<br />
 **[[1oyv]] – BsSub+tomato inhibitor II<br />
@@ Line 77: / Line 73: @@
 **[[1av7]], [[1avt]], [[3vsb]], [[1vsb]] – BsSub+boronic acid derivatives <br />
 **[[1scn]] – BsSub+carbamate derivative <br />
-**[[1bh6]] – Sub DY+benzyloxycarbonyl-ala-pro-phe-chloromethyl ketone – ''Bacillus licheniformis''<br />
+**[[1bh6]] – BliSub DY+benzyloxycarbonyl-ala-pro-phe-chloromethyl ketone – ''Bacillus licheniformis''<br />
-**[[2wuv]], [[2wuw]] – BlSub fragment+acetonitrile<br />
+**[[2wuv]], [[2wuw]] – BliSub fragment+acetonitrile<br />
-**[[4c3u]] – BlSub + Ca + Cs<br />
+**[[4c3u]] – BliSub + Ca + Cs<br />
-**[[4c3v]] – BlSub + Ca <br />
+**[[4c3v]] – BliSub + Ca <br />
 *Selenosubtilisin
@@ Line 89: / Line 85: @@
 *Savinase
-**[[3bx1]], [[1svn]], [[4cfy]], [[4cfz]], [[4cg0]] – Sav – ''Bacillus lentus''
+**[[3bx1]], [[1svn]], [[4cfy]], [[4cfz]], [[4cg0]][[1iav]], [[1gci]], [[1jea]], [[1st3]] – 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/>
 [[Category:Topic Page]]