Subtilisin: Difference between revisions

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{{STRUCTURE_2z2x|  PDB=2z2x  | SIZE=400| SCENE=Subtilisin/Cv/1 |right|CAPTION=Subtilisin with monoisopropylphosphorylserine complex with Ca+2 ions (green) [[2z2x]] }}
<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 ==
[[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]].


[[Subtilisin]] is a serine protease.  It is widely used commercially in detergents.
*'''Selenosubtilisin''' is a semisynthetic selenoenzyme produced by chemical modification of subtilisin<ref>PMID:8385489</ref>.<br />
A 77 amino acid propeptide is cleaved from the N-terminus of pro-Sub to create the mature active enzyme.  See detalis in [[User:Tommie Hata/Introduction to Protein Engineering-Subtilisin]].
*'''Savinase''' is a subtilisin produced from a lentil<ref>PMID:24738747</ref>.<br />


== 3D Structures of Subtilisin ==
== Relevance ==
Subtilisin is widely used commercially in detergents.


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
== Structural highlights ==
{{#tree:id=OrganizedByTopic|openlevels=0|
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>.


* Native mature subtilisin
== 3D Structures of Subtilisin ==
 
[[Subtilisin 3D structures]]
**[[2z2x]] – TkSub  - ''Thermococcus kodakarensis''<br />
**[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub  - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br />
**[[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''
 
* Mutant mature subtilisin
 
**[[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 />
 
* Unautoprocessed subtilisin (pro-Sub)
 
**[[2z2z]], [[2e1p]] – pro-TkSub <br />
**[[2zwo]], [[2zwp]], [[4jp8]], [[3wiu]], [[3wiv]] – pro-TKSub  (mutant)<br />
**[[2wv7]] – pro-BcSub <br />
**[[2wwt]], [[2x8j]] - pro-BcSub (mutant)<br />
**[[3whi]] - pro-BcSub (mutant)<br />
 
* Mutant unautoprocessed subtilisin
 
**[[2zwo]], [[2zwp]] – pro-TKSub
 
* Mature subtilisin complexed with its propeptide
 
**[[3cnq]] – BaSub<br />
**[[1spb]] – BaSub (mutant)<br />
**[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub<br />
**[[3vv2]] – TkSub (mutant)<br />
**[[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<br />
**[[1tm5]], [[1tm7]], [[1tmg]], [[1to1]], [[1to2]] - BaSub+ chymotrypsin inhibitor 2 (mutant)<br />
**[[3sic]], [[5sic]], [[2sic]] – BaSub+Streptomyces inhibitor SSI<br />
**[[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 />
**[[1sbn]], [[1sib]], [[2sec]], [[1sni]], [[1cse]] – BsSub+Elgin C<br />
**[[2sni]] - BaSub+Elgin C2 <br />
**[[1mee]] - BpSub+Elgin C – ''Bacillus pumilus''
 
* Subtilisin complexed with inhibitor
 
**[[3bgo]] – BaSub+azide <br />
**[[1c3l]] – BsSub+Xe<br />
**[[1be8]] – BsSub+cinnamoyl<br />
**[[1be6]] - BsSub+cinnamoyl+acetonitrile<br />
**[[1bfk]], [[1scd]] – BsSub+acetonitrile<br />
**[[1bfu]], [[1af4]] – BsSub+dioxane<br />
**[[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 />
**[[2wuv]], [[2wuw]] – BlSub fragment+acetonitrile<br />
**[[4c3u]] – BlSub + Ca + Cs<br />
**[[4c3v]] – BlSub + Ca <br />
 
*Selenosubtilisin
 
**[[1ubn]] – BaSel-Sub<br />
**[[1sel]] – BsSel-Sub


*Savinase
</StructureSection>


**[[3bx1]], [[1svn]], [[4cfy]], [[4cfz]], [[4cg0]] – Sav – ''Bacillus lentus''
== References ==
}}
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:53, 14 August 2024

Function

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[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].

3D Structures of Subtilisin

Subtilisin 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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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Alexander Berchansky, Michal Harel, Joel L. Sussman
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