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Subtilisin information


Peptidase S8, subtilisin-related
S8 + I9 (lower-right), Bacillus subtilis (PDB: 2pmw​)
Identifiers
SymbolPeptidase_S8
PfamPF00082
InterProIPR015500
PROSITEPDOC00125
CATH1cse
SCOP21cse / SCOPe / SUPFAM
CDDcd07477
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Subtilisin BPN'
Crystal structure of subtilisin S8 domain.[1]
Identifiers
OrganismBacillus amyloliquefaciens
Symbolapr
CAS number9014-01-1
Entrez5712479
PDB1st2 More structures
UniProtP00782
Other data
EC number3.4.21.62
Search for
StructuresSwiss-model
DomainsInterPro
GO:0004252

Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis.[2][3][4][5][6][7][8]

Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, Bacillus amyloliquefaciens from which they are secreted in large amounts.

  1. ^ PDB: 1st2​; Bott R, Ultsch M, Kossiakoff A, Graycar T, Katz B, Power S (June 1988). "The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 A and an analysis of the structural consequences of peroxide inactivation". The Journal of Biological Chemistry. 263 (16): 7895–906. doi:10.1016/S0021-9258(18)68582-5. PMID 3286644.
  2. ^ Ottesen M, Svendsen I (1970). The subtilisins. Methods Enzymol. Vol. 19. pp. 199–215. doi:10.1016/0076-6879(70)19014-8. ISBN 978-0-12-181881-4.
  3. ^ Markland FS, Smith EL (1971). "Subtilisins: primary structure, chemical and physical properties". In Boyer PD (ed.). The Enzymes. Vol. 3 (3rd ed.). New York: Academic Press. pp. 561–608.
  4. ^ Philipp M, Bender ML (1983). "Kinetics of subtilisin and thiolsubtilisin". Molecular and Cellular Biochemistry. 51 (1): 5–32. doi:10.1007/bf00215583. PMID 6343835. S2CID 24136200.
  5. ^ Nedkov P, Oberthür W, Braunitzer G (April 1985). "Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus". Biological Chemistry Hoppe-Seyler. 366 (4): 421–30. doi:10.1515/bchm3.1985.366.1.421. PMID 3927935.
  6. ^ Ikemura H, Takagi H, Inouye M (June 1987). "Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli". The Journal of Biological Chemistry. 262 (16): 7859–64. doi:10.1016/S0021-9258(18)47646-6. PMID 3108260.
  7. ^ Polgár L (1987). "Structure and function of serine proteases". In Brocklehurst K, Neuberger A (eds.). Hydrolytic enzymes. Amsterdam: Elsevier. ISBN 0-444-80886-8.
  8. ^ Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D (September 1984). "Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein". Journal of Bacteriology. 159 (3): 811–9. doi:10.1128/JB.159.3.811-819.1984. PMC 215730. PMID 6090391.

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Subtilisin

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Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis. Subtilisins belong to subtilases, a group of serine proteases...

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Serine protease

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categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. The MEROPS protease classification system counts 16 superfamilies...

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PCSK9

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Proprotein convertase subtilisin/kexin type 9 (PCSK9) is an enzyme encoded by the PCSK9 gene in humans on chromosome 1. It is the 9th member of the proprotein...

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Nattokinase

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(and should not be pronounced as such), but a serine protease of the subtilisin family (99.5% identical with aprE). Rather, it is named for the fact that...

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Klenow fragment

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DNA polymerase I from E. coli is enzymatically cleaved by the protease subtilisin. First reported in 1970, it retains the 5' → 3' polymerase activity and...

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Furin

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family S8, furin is a subtilisin-like peptidase. The protein encoded by this gene is an enzyme that belongs to the subtilisin-like proprotein convertase...

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Proprotein convertase 1

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substrate). It is related to the bacterial enzyme known as subtilisin. There are nine subtilisin homologs in mammals; in addition to proprotein convertase...

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Structural Classification of Proteins database

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Searching for "Subtilisin" returns the protein, "Subtilisin from Bacillus subtilis, carlsberg", with the following lineage. Subtilisin from Bacillus subtilis...

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Evolocumab

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a fully human monoclonal antibody that inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9). PCSK9 is a protein that targets LDL receptors for...

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Coprophagia

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bacterial dysentery; its efficacy (probably attributable to the antibiotic subtilisin from Bacillus subtilis) was anecdotally confirmed by German soldiers in...

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Subtilase

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Subtilases are a family of subtilisin-like serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad...

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Boronic acid

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site serines and are part of inhibitors for porcine pancreatic lipase, subtilisin and the protease Kex2. Furthermore, boronic acid derivatives constitute...

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Protein

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Ottesen M, Richards FM (February 1955). "Degradation of ribonuclease by subtilisin". Biochimica et Biophysica Acta. 16 (2): 297–299. doi:10.1016/0006-3002(55)90224-9...

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Bacillus licheniformis

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licheniformis one of the most important bacteria in industrial enzyme production. Subtilisin Carlsberg (P00780) secreted by B. licheniformis is used as a detergent...

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Convergent evolution

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organisation of acid-base-nucleophile in different protease superfamilies. Shown are the triads of subtilisin, prolyl oligopeptidase, TEV protease, and papain....

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Taraxacum

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O.; Dunaevsky, Y. E.; Golovkin, B. N.; Stepanov, V. M. (1999). "A new subtilisin-like proteinase from roots of the dandelion Taraxacum officinale Webb...

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SSI protease inhibitor

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In molecular biology the protein SSI is a Subtilisin inhibitor-like which stands for Streptomyces subtilisin inhibitor. This is a protease inhibitor. These...

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Proteinase K

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for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons (28.9 kDa). Activated...

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Bacillus

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production of alpha amylase used in starch hydrolysis and the protease subtilisin used in detergents. B. subtilis is a valuable model for bacterial research...

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List of biophysically important macromolecular crystal structures

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preventing the enzyme from sucking in the chain past the first residue. 1969 – Subtilisin (PDB file 1sbt ) was a second type of serine protease with a near-identical...

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Inclisiran

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specifically, inhibiting translation of the protein termed proprotein convertase subtilisin/kexin type 9 (PCSK9). Small interfering RNA molecules (siRNAs) are designed...

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Industrial enzymes

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Digestive aid Urokinase Pharmaceutical Anticoagulant β-Lactamase Pharmaceutical Penicillin allergy treatment Subtilisin Consumer Goods Laundry detergent...

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Taraxacum officinale

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O.; Dunaevsky, Y. E.; Golovkin, B. N.; Stepanov, V. M. (1999). "A new subtilisin-like proteinase from roots of the dandelion Taraxacum officinale Webb...

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Proopiomelanocortin

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extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. The encoded protein is synthesized...

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Frances Arnold

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work, published in 1993, she used the method to engineer a version of subtilisin E that was active in the organic solvent DMF, a highly unnatural environment...

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Proteolysis

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similar strategy of employing an inactive zymogen or prezymogen is used. Subtilisin, which is produced by Bacillus subtilis, is produced as preprosubtilisin...

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Wound

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Examples include trypsin, streptokinase-streptodornase combination, subtilisin, papain, and collagenase. Surgical Debridement: Also known as sharp debridement...

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