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Proteolytic enzyme found in Bacillus subtilis
Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis. Subtilisins belong to subtilases, a group of serine proteases
Subtilisin
Mammalian protein found in humans
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
PCSK9
Protease commonly found in natto
This enzyme is known as subtilisin NAT (S08.044) in the MEROPS database. Synonyms include nattokinase, subtilisin QK, subtilisin QK02. The gene encodes
Nattokinase
Class of enzymes
categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. The MEROPS protease classification system counts 16 superfamilies
Serine_protease
Protein family
In molecular biology the protein SSI is a Subtilisin inhibitor-like which stands for Streptomyces subtilisin inhibitor. This is a protease inhibitor. These
SSI_protease_inhibitor
Protein-coding gene in the species Homo sapiens
Proprotein convertase subtilisin/kexin type 6 is an protease that in humans is encoded by the PCSK6 gene which is located in chromosome 15. Pcsk6 is a
PCSK6
Pathogenic type of misfolded protein
sp, subtilisin-like pernisine from Aeropyrum pernix, alkaline protease from Nocardiopsis sp, nattokinase from B. subtilis, engineered subtilisins from
Prion
Biological database of proteins
Searching for "Subtilisin" returns the protein, "Subtilisin from Bacillus subtilis, carlsberg", with the following lineage. Subtilisin from Bacillus subtilis
Structural Classification of Proteins database
Structural_Classification_of_Proteins_database
Pharmaceutical drug
treatment of hyperlipidemia. Evolocumab inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9). PCSK9 is a protein that targets LDL receptors for
Evolocumab
Prohormone-processing protease
killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases
Kexin
Enzyme found in humans
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
Furin
Large protein fragment
polymerase I (Pol I) from E. coli is enzymatically cleaved by the protease subtilisin. First reported in 1970, it retains the 5' → 3' polymerase activity and
Klenow_fragment
Species of bacterium
licheniformis one of the most important bacteria in industrial enzyme production. Subtilisin Carlsberg (P00780) secreted by B. licheniformis is used as a detergent
Bacillus_licheniformis
substrate). It is related to the bacterial enzyme known as subtilisin. There are nine subtilisin homologs in mammals; in addition to proprotein convertase
Proprotein_convertase_1
Set of three coordinated amino acids
Simultaneously, the structures of the evolutionarily unrelated papain and subtilisin proteases were found to contain analogous triads. The 'charge-relay' mechanism
Catalytic_triad
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
List of biophysically important macromolecular crystal structures
List_of_biophysically_important_macromolecular_crystal_structures
Organic compound of the form R–B(OH)2
site serines and are part of inhibitors for porcine pancreatic lipase, subtilisin and the protease Kex2. Furthermore, boronic acid derivatives constitute
Boronic_acid
Independent evolution of similar features
organisation of acid-base-nucleophile in different protease superfamilies. Shown are the triads of subtilisin, prolyl oligopeptidase, TEV protease, and papain.
Convergent_evolution
Pharmaceutical compound
is a recombinant fusion protein that contains a proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor and human serum albumin. Lerodalcibep was
Lerodalcibep
Mammalian protein found in Homo sapiens
Proprotein convertase subtilisin/kexin type 1 inhibitor is a protein by the name of proSAAS that in humans is encoded by the PCSK1N gene. This protein
Proprotein convertase subtilisin/kexin type 1 inhibitor
Proprotein_convertase_subtilisin/kexin_type_1_inhibitor
Phytaspase is a member of the plant subtilisin-like protease family, and is commonly distinguished from the other members by its unusual and extremely
Phytaspase
Biomolecule consisting of chains of amino acid residues
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
Protein
American chemist and academic (born 1956)
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
Frances_Arnold
Protein family
Subtilases are a family of subtilisin-like serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad
Subtilase
Pharmaceutical drug
Inclisiran inhibits translation of the protein termed proprotein convertase subtilisin/kexin type 9 (PCSK9). Small interfering RNA molecules (siRNAs) are designed
Inclisiran
Genus of bacteria
production of alpha amylase used in starch hydrolysis and the protease subtilisin used in detergents. B. subtilis is a valuable model for bacterial research
Bacillus
Protein family
domain at the N-terminus of peptidases belonging to MEROPS family S8A, subtilisins. The propeptide is removed by proteolytic cleavage; removal activating
Protease_inhibitor_(biology)
Genus of flowering plants in the family Asteraceae
2019. Bogacheva AM, Rudenskaya GN, Preusser A, et al. (1999). "A new subtilisin-like proteinase from roots of the dandelion Taraxacum officinale Webb
Taraxacum
Protein-coding gene in the species Homo sapiens
gene. It is related to the bacterial enzyme subtilisin, and altogether there are 9 different subtilisin-like genes in mammals: furin, PACE4, PC4, PC5/6
Proprotein_convertase_2
Technique in molecular biology
application. For example, commonly used laundry detergents may contain subtilisin, whose wild-type form has a methionine that can be oxidized by bleach
Site-directed_mutagenesis
American biochemist
enzyme action. He also studied artificial enzymes, starting with modified subtilisin in which a serine residue was replaced by cysteine (replacing an ester
Myron_L._Bender
Process of removing a mark or spot
stains. One of the most intensively studied protease for this purpose is subtilisin. Baby powder This can be used to absorb grease before washing, especially
Stain_removal
Breakdown of proteins into smaller polypeptides or amino acids
similar strategy of employing an inactive zymogen or prezymogen is used. Subtilisin, which is produced by Bacillus subtilis, is produced as preprosubtilisin
Proteolysis
Class of enzymes
aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor". Bioscience
Aqualysin_1
Broad-spectrum serine protease
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
Proteinase_K
Examples of separate lineages of organisms developing similar characteristics
organisation of acid-base-nucleophile in different protease superfamilies. Shown are the triads of subtilisin, prolyl oligopeptidase, TEV protease, and papain.
List of examples of convergent evolution
List_of_examples_of_convergent_evolution
Low-density lipoprotein containing apolipoprotein(a)
interfering RNAs (such as Pelacarsen and Olpasiran), and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors. The American Academy of Pediatrics now
Lipoprotein(a)
Mammalian protein found in Homo sapiens
extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. The POMC gene is expressed
Proopiomelanocortin
Chemical compound
Whole antibody Source Humanized (from mouse) Target Proprotein convertase subtilisin/kexin type 9 (PCSK9) Clinical data Routes of administration Subcutaneous
Bococizumab
American biochemist (1920–2007)
chemical modification to change the serine residue in the active site of subtilisin to cysteine, (in parallel with a similar experiment done independently
Daniel_E._Koshland_Jr.
Process of transplantation of fecal bacteria from a healthy individual into a recipient
bacterial dysentery; its efficacy, probably attributable to the antimicrobial subtilisin produced by Bacillus subtilis, was anecdotally confirmed by German soldiers
Fecal_microbiota_transplant
Protein-coding gene in the species Homo sapiens
Proprotein convertase subtilisin/kexin type 5 is an enzyme that in humans is encoded by the PCSK5 gene, found in chromosome 9q21.3 Two alternatively spliced
PCSK5
Flowering plant species known as dandelion
O.; Dunaevsky, Y. E.; Golovkin, B. N.; Stepanov, V. M. (1999). "A new subtilisin-like proteinase from roots of the dandelion Taraxacum officinale Webb
Taraxacum_officinale
Part of an egg which feeds the developing embryo
Willebrand factor type D domain at the C-terminal. Additionally, it features a subtilisin-like cleavage site, a trait shared with apoLp-II/I. Evolutionary analyses
Yolk
Biological catalysts used in production
Digestive aid Urokinase Pharmaceutical Anticoagulant β-Lactamase Pharmaceutical Penicillin allergy treatment Subtilisin Consumer Goods Laundry detergent
Industrial_enzymes
Disruption or damage to living tissue
Examples include trypsin, streptokinase-streptodornase combination, subtilisin, papain, and collagenase. Surgical debridement: Also known as sharp debridement
Wound
British biochemist and academic
Institutions University of Cambridge Harvard University Thesis Studies on subtilisin BPN' and chymotrypsin inhibitor 2 (1991) Doctoral advisor Alan Fersht
Sophie_E._Jackson
Protein-coding gene in the species Homo sapiens
Proprotein convertase subtilisin/kexin type 4 is an enzyme that in humans is encoded by the PCSK4 gene. GRCh38: Ensembl release 89: ENSG00000115257 – Ensembl
PCSK4
Type of secondary structure of proteins
acids, and drug molecules – many of which featuring α-helices, such as subtilisin, human growth hormone, and phospholipase A2. Mike Tyka is a computational
Alpha_helix
hydrolases includes: Serine proteases, including trypsin, chymotrypsin, and subtilisin Extracellular lipases, including pancreatic lipase, hepatic lipase, gastric
Serine_hydrolase
Index of enzymes associated with the same name
Subtilopeptidase A may refer to: Subtilisin, EC 3.4.21.62 Oryzin, EC 3.4.21.63 Proteinase K, EC 3.4.21.64 Thermomycolin, EC 3.4.21.65 Thermitase, EC 3
Subtilopeptidase_A
Species of fungus
significant expansion of genes encoding secreted proteins, including subtilisins, chitinases, and carboxypeptidases, which assist in degrading nematode
Pochonia_chlamydosporia
Species of fungus
healthy nematodes, and it was later determined that a paralyzing substance, Subtilisin (A serine protease), is excreted into nematodes. An unstable toxin was
Arthrobotrys_oligospora
Protein found in egg whites
third Kazal domain of the turkey ovomucoid protein (orange) bound to subtilisin Carlsberg, a serine protease. Identifiers Organism Meleagris gallopavo
Ovomucoid
from pancreatic ribonuclease A (RNase A). If RNase A is digested with subtilisin, a single peptide bond is cleaved, but the resulting two products remain
S-tag
Scientific study of lipids
bloodstream—is an option. Pharmacologic inhibition of proprotein convertase subtilisin/kexin type 9 (PCSK9), an enzyme crucial for maintaining lipoprotein homeostasis
Lipidology
Proteolytic enzyme that digests keratin
al., 1998 and Bressollier et al., 1999). Some are more specifically subtilisins. Being a functional classification, there is not necessarily a shared
Keratinase
Genus of archaea
kodakarensis has four virus-like integrated gene elements containing subtilisin-like serine protease precursors. To date, only two viruses have been isolated
Thermococcus
Chemical compound
protein bound lipoic acid released 1.4−11.6 ng/mL and <1-38.2 ng/mL using subtilisin and alcalase, respectively. Digestive proteolytic enzymes cleave the R-lipoyllysine
Lipoic_acid
Mammalian protein found in Homo sapiens
factor site-1 protease, or site-1 protease (S1P) for short, also known as subtilisin/kexin-isozyme 1 (SKI-1), is an enzyme (EC 3.4.21.112) that in humans is
Membrane-bound transcription factor site-1 protease
Membrane-bound_transcription_factor_site-1_protease
High levels of cholesterol in the blood
Tantry U, Lin Y, et al. (July 2015). "Effects of Proprotein Convertase Subtilisin/Kexin Type 9 Antibodies in Adults With Hypercholesterolemia: A Systematic
High_cholesterol
Biological enzymes that are used as laundry detergents
of laundry enzymes is Bacillus subtilis, which produces the protease subtilisin. For stain removal, conventional household washing machines use heated
Detergent_enzymes
Family of RNA viruses
reactions are catalysed by cellular signal peptidases and the cellular enzyme Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P). These processes are essential
Arenavirus
American biochemist and microbiologist (1938–2025)
DNA polymerase I in which the 5'-exonuclease had been inactivated by subtilisin. The polymerization with the primer annealed to the template generated
Clyde_A._Hutchison_III
Study of biochemical reaction rates catalysed by an enzyme
hydrolytic enzyme solutions: alpha-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesterase". Journal of the American Chemical Society.
Enzyme_kinetics
Class of insect proteins
cleavage (furin). Furin is a member of the proprotein convertase family of subtilisin like serine endoproteases that is mainly active in the trans-Golgi network
Lipophorin
Angle in physical organic chemistry
value determined for enzymatic cleavage of an amide by a serine protease (subtilisin) was 88°, quite distinct from the hydride-formaldehyde value of 107°;
Bürgi–Dunitz_angle
Transfer of genes from unrelated organisms
insights into the evolution and structure of Colletotrichum plant-like subtilisins (CPLSs)". Communicative & Integrative Biology. 6 (6) e25727. doi:10.4161/cib
Horizontal_gene_transfer
Pharmaceutical drug
antibody Type Whole antibody Source Human Target Proprotein convertase subtilisin/kexin type 9 (PCSK9) Clinical data Trade names Praluent AHFS/Drugs.com
Alirocumab
Species of bacterium
often used in starch hydrolysis. B. amyloliquefaciens is also a source of subtilisin, which catalyzes the breakdown of proteins in a similar way to trypsin
Bacillus_amyloliquefaciens
Class of enzymes
Manual Than and Wolfram Bode. The key features of Kex2 and Furin are a subtilisin-related catalytic domain, a specificity pocket that requires the amino
Proprotein_convertase
Enzyme
A (2011). "Molecular Cloning and Expression of Cucumisin (Cuc m 1), a Subtilisin-like Protease of Cucumis melo in Escherichia coli". Allergology International
Cucumisin
Genus of fungi
crispa (Wulf.) and Their Inhibitory Activities on Proprotein Convertase Subtilisin/Kexin Type 9 mRNA Expression". J. Agric. Food Chem. 65 (30): 6152–6157
Sparassis
Protein engineering method
Engineering for Nonaqueous Solvents: Random Mutagenesis to Enhance Activity of Subtilisin E in Polar Organic Media". Bio/Technology. 9 (11): 1073–1077. doi:10.1038/nbt1191-1073
Directed_evolution
Class of enzymes
was discovered in 1976. Exposure of DNA polymerase I to the protease subtilisin cleaves the molecule into a smaller fragment, which retains only the DNA
DNA_polymerase_I
Protein domain
peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin")
Sedolisin
Chemical compound
genetic conditions: pro-opiomelanocortin (POMC) deficiency, proprotein subtilisin/kexin type 1 (PCSK1) deficiency, and leptin receptor (LEPR) deficiency
Setmelanotide
Species of fungus
acremostrictin presents as a colorless crystal solid. AsES (S. strictum elicitor subtilisin; R4IR27) protein is an extracellular elicitor protein produced by S. strictum
Sarocladium_strictum
Chemical reaction intermediate
(1986). "Site-directed mutagenesis and the role of the oxyanion hole in subtilisin". Proc. Natl. Acad. Sci. USA. 83 (11): 3743–5. Bibcode:1986PNAS...83.3743B
Tetrahedral carbonyl addition compound
Tetrahedral_carbonyl_addition_compound
Ribonuclease S, which is RNase A that has been treated with the protease subtilisin, was the third protein to have its crystallographic structure solved,
Bovine pancreatic ribonuclease
Bovine_pancreatic_ribonuclease
Dependence of a gene mutation's phenotype on mutations in other genes
Koshland DE (November 1966). "The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation"". Proceedings of the National Academy
Epistasis
Genus of archaea
Baumeister W, Peters J (1996). "A hyperthermostable protease of the subtilisin family bound to the surface layer of the Archaeon Staphylothermus marinus"
Staphylothermus
Enzyme encoded by hepatitis C virus
inhibit the protease mechanism. Inhibitors for protease such as Papain, Subtilisin and one from Sindbis virus capsid might share some similarities as they
NS2-3_protease
Protein found in humans
Müller E (February 2003). "Novel insights into cadherin processing by subtilisin-like convertases". FEBS Letters. 536 (1–3): 203–8. doi:10.1016/S0014-5793(02)03897-8
Desmoglein-3
Protein-coding gene in humans
convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene. The protein encoded by this gene belongs to the subtilisin-like
PCSK7
American chemical biologist and protein engineer
his group pioneered "gain-of-function engineering" of enzymes (such as subtilisin), growth factors (human growth hormone), and antibodies by site-directed
James_A._Wells
Genetic disorder characterized by high cholesterol levels
severity of the hypercholesterolemia. Mutations in the proprotein convertase subtilisin/kexin type 9 (PCSK9) gene were linked to autosomal dominant (i.e. requiring
Familial_hypercholesterolemia
Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases". FEBS Lett. 183 (2): 195–200. Bibcode:1985FEBSL.183
Thermitase
4.4.16: Now covered by the microbial serine proteinases EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64 (endopeptidase K), EC 3.4.21.65
List_of_EC_numbers_(EC_3)
Species of fungus
Sub2, which encode the proteases carboxypeptidase, ceraminidase, and subtilisin, respectively. Among other virulence-related enzymes, T. tonsurans also
Trichophyton_tonsurans
Protein-coding gene in the species Homo sapiens
Tsoi LC, Le ST, Luxardi G, et al. (August 2022). "Proprotein convertase subtilisin/kexin type 9 is a psoriasis-susceptibility locus that is negatively related
IL36G
secondary cleavage site at Ala58-Ser59. This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate preference. Wexler
C5a_peptidase
Topics referred to by the same term
Thermoase may refer to: Subtilisin, an enzyme Thermolysin, an enzyme This disambiguation page lists articles associated with the title Thermoase. If an
Thermoase
Protein-coding gene in the species Homo sapiens
Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48. 2q36: Actin Dimer Cross-linked between Residues
ACTA2
Medical condition
deficiency, Wolfram syndrome (WFS1 gene mutation), and proprotein convertase subtilisin/kexin type 1 (PCSK1) gene deficiency. The main mutations are associated
Central_diabetes_insipidus
Topics referred to by the same term
2017–2019 Peugeot Type 9, an automobile built 1894–1897 Proprotein convertase subtilisin/kexin type 9, a protein found in humans All pages with titles containing
Type_9_(disambiguation)
Chemical washing process
1016/S0959-6526(03)00074-X. Lin, Jianhua (1999). Protease (chymotrypsin, Subtilisin) Scouring of Raw Cotton and Fabric Physical Properties: Effects of Pretreatment
Scouring_(textiles)
enzymes. Such proteases range from pepsin, trypsin, alpha-chymotrypsin, subtilisin, pronase E, bromelin, proteinase K, alpha-amylase, and pancreatin. The
Phallolysin
American chemist (1911 - 1995)
analytical cases. In 1959, Fred Richards discovered that a proteolytic enzyme, Subtilisin, had the ability to cleave the enzyme Ribonuclease A into two components
Klaus_H._Hofmann
syndrome PR-6 IPR000864 Potato protease I Proteinase inhibitor PR-7 (Subtilisin-like) Tomato endoproteinase P69 (O82007) Endoproteinase PR-8 (GH18) Cucumber
Pathogenesis-related_protein
SUBTILISIN
SUBTILISIN
SUBTILISIN
SUBTILISIN
Girl/Female
Hindu, Indian
Gift of God
Boy/Male
Indian, Punjabi, Sikh
Love of Rays
Boy/Male
Danish, German, Swedish
God is Merciful; Established by God
Girl/Female
Tamil
Sanjushree | ஸஂஜà¯à®·à¯à®°à¯€
Beautiful
Boy/Male
Indian, Sanskrit
Lotus Eyed
Girl/Female
Arabic
Jupiter
Surname or Lastname
English
English : variant spelling of Painter.
Girl/Female
Indian
Somebody who gives shelter, Goddess Lakshmi
Girl/Female
Arabic
Friday
Girl/Female
Australian, German, Polish
Healthy; Strong
SUBTILISIN
SUBTILISIN
SUBTILISIN
SUBTILISIN
SUBTILISIN