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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>. |
| | |
| | == 3D Structures of Subtilisin == |
| | [[Subtilisin 3D structures]] |
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| </StructureSection> | | </StructureSection> |
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| **[[2z2x]] – TkSub - ''Thermococcus kodakarensis''<br /> | | **[[2z2x]] – TkSub - ''Thermococcus kodakarensis''<br /> |
| **[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br /> | | **[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br /> |
| | **[[6pak]] - BsSub E (mutant)<br /> |
| **[[1pxq]] – BsSub - NMR<br /> | | **[[1pxq]] – BsSub - NMR<br /> |
| **[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub - ''Bacillus amyloliquefaciens''<br /> | | **[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub - ''Bacillus amyloliquefaciens''<br /> |
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| * Mature subtilisin complexed with its propeptide | | * Mature subtilisin complexed with its propeptide |
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| **[[3cnq]] – BaSub<br /> | | **[[3cnq]], [[5ox2]] – BaSub + prodomain<br /> |
| **[[1spb]] – BaSub (mutant)<br /> | | **[[1spb]] – BaSub (mutant) + prodomain<br /> |
| **[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub<br /> | | **[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub + prodomain<br /> |
| **[[3vv2]] – TkSub (mutant)<br /> | | **[[3vv2]] – TkSub (mutant) + prodomain<br /> |
| **[[1scj]] – BsSub | | **[[1scj]] – BsSub + prodomain<br /> |
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| * Subtilisin complexed with polypeptide inhibitor | | * Subtilisin complexed with polypeptide inhibitor |
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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].
3D Structures of Subtilisin
Subtilisin 3D structures
- ↑ 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:https://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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3D Structures of Subtilisin
Updated on 10-February-2020
{"openlevels":0}
- Native mature subtilisin
- 2z2x – TkSub - Thermococcus kodakarensis
- Subtilisin 3D structures, 1scb, 1sbc, 3unx – BsSub - Bacillus subtilis (Subtilisin Carlsberg)
- 6pak - BsSub E (mutant)
- 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)
- Mature subtilisin complexed with its propeptide
- 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
- 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
References
