Subtilisin
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
<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'> | <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 == | == Function == | ||
| - | [[Subtilisin]] is a serine protease. A | + | [[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]]. |
*'''Selenosubtilisin''' is a semisynthetic selenoenzyme produced by chemical modification of subtilisin<ref>PMID:8385489</ref>.<br /> | *'''Selenosubtilisin''' is a semisynthetic selenoenzyme produced by chemical modification of subtilisin<ref>PMID:8385489</ref>.<br /> | ||
| Line 17: | Line 17: | ||
</StructureSection> | </StructureSection> | ||
| - | == 3D Structures of Subtilisin == | ||
| - | |||
| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | |||
| - | * Native mature subtilisin | ||
| - | |||
| - | **[[2z2x]] – TkSub - ''Thermococcus kodakarensis''<br /> | ||
| - | **[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br /> | ||
| - | **[[6pak]] - BsSub E (mutant)<br /> | ||
| - | **[[1pxq]] – BsSub - NMR<br /> | ||
| - | **[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub - ''Bacillus amyloliquefaciens''<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 /> | ||
| - | **[[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 /> | ||
| - | |||
| - | * Mature subtilisin complexed with its propeptide | ||
| - | |||
| - | **[[3cnq]], [[5ox2]] – BaSub + prodomain<br /> | ||
| - | **[[1spb]] – BaSub (mutant) + prodomain<br /> | ||
| - | **[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub + prodomain<br /> | ||
| - | **[[3vv2]] – TkSub (mutant) + prodomain<br /> | ||
| - | **[[1scj]] – BsSub + prodomain<br /> | ||
| - | |||
| - | * 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 /> | ||
| - | **[[1r0r]] – BsSub+ovomucoid<br /> | ||
| - | **[[1oyv]] – BsSub+tomato inhibitor II<br /> | ||
| - | **[[1sbn]], [[1sib]], [[2sec]], [[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]] – BliSub DY+benzyloxycarbonyl-ala-pro-phe-chloromethyl ketone – ''Bacillus licheniformis''<br /> | ||
| - | **[[2wuv]], [[2wuw]] – BliSub fragment+acetonitrile<br /> | ||
| - | **[[4c3u]] – BliSub + Ca + Cs<br /> | ||
| - | **[[4c3v]] – BliSub + Ca <br /> | ||
| - | |||
| - | * Selenosubtilisin | ||
| - | |||
| - | **[[1ubn]] – BaSel-Sub<br /> | ||
| - | **[[1sel]] – BsSel-Sub | ||
| - | |||
| - | * Savinase | ||
| - | |||
| - | **[[3bx1]], [[1svn]], [[4cfy]], [[4cfz]], [[4cg0]], [[1iav]], [[1gci]], [[1jea]], [[1st3]], [[5aqe]], [[5arb]], [[5arc]], [[5ard]] – 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 == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
| |||||||||||
References
- ↑ 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
