3.4.21.62: Subtilisin
This is an abbreviated version!
For detailed information about Subtilisin, go to the full flat file.
Reaction
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
=
Synonyms
AcpII, Ak.1 protease, Alcalase, Alcalase 0.6L, Alcalase 2.5L, ALE1 subtilase, ALK-enzyme, Alkaline mesentericopeptidase, Alkaline protease, alkaline serine protease, ALP1, Alzwiprase, aprE, AprE51, aqualysin, Arp, AsES, Asp v 13, AtSBT1.9, Bacillopeptidase A, Bacillopeptidase B, Bacillus gibsonii alkaline protease, Bacillus subtilis alkaline proteinase Bioprase, BgAP, Bioprase AL 15, Bioprase APL 30, BLS, BPN', BprB, BprV, C1 subtilase, cold active subtilisin-like serine proteinase, Colistinase, EC 3.4.21.14, EC 3.4.4.16, Esperase, Fe protease, Fe prtS8A, Genenase I, intracellular subtilisin protease, ISP, IvaP, Kazusase, Maxatase, mesenteroicopeptidase, More, Nagarse, Opticlean, ORF2, Orientase 10B, P69 subtilase, PBANKA_1106900, PbSOPT, Peptidase, subtilo-, A, PF3D7_0507300, phytophase, PIMMS2, Protease S, Protease VIII, Protease XXVII, Proteinase K, Proteinase, Bacillus subtilis alkaline, Protin A 3L, PSP-3, psychrophilic subtilisin-like protease, S1P subtilase, SAP, SAS-1, SASP, saspase, Savinase, Savinase 16.0L, Savinase 32.0 L EX, Savinase 4.0T, Savinase 8.0L, savinaseTM, SBc, SBL, SDD1 subtilase, senescence-associated subtilisin protease, SES7, SISBT3 subtilase, SOPT, SP 266, Sspa, SSU0757, SUB1, SUB2, subC, subtilase, subtilase subfamily 1 member 9, subtilase-like protease, subtilisin, subtilisin 72, subtilisin A, Subtilisin amylosacchariticus, Subtilisin BL, subtilisin BPN’, subtilisin C., subtilisin Carlsberg, subtilisin DJ-4, Subtilisin DY, Subtilisin E, subtilisin E-S7, Subtilisin GX, subtilisin JB1, subtilisin Karlsberg, Subtilisin Novo, subtilisin Pr1-like protease, subtilisin protease, subtilisin QK, Subtilisin S41, subtilisin S4I, subtilisin S88, Subtilisin Sendai, subtilisin Sph, subtilisin-like ookinete protein, subtilisin-like ookinete protein important for transmission, subtilisin-like protease, subtilisin-like protease AprV2, subtilisin-like serine protease, Subtilisn J, Subtilopeptidase, Superase, thermitase, thermo-active subtilisin-like serine protease, Thermoase, Thermoase PC 10, thermophilic thermitase, thermostable subtilisin, ThSS45, Tk-subtilisin, trans-cinnamoyl-subtilisin, V. cholerae-secreted serine protease, VC_0157, vPR
ECTree
Application
Application on EC 3.4.21.62 - Subtilisin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
degradation
-
subtilisin releases Phr signalling peptides derived from the C-terminus of their precursor proteins, but does not release Phr peptides derived from an internal portion of its precursor proteins
food industry
-
alcalase-hydrolyzed potato protein has both antioxidant and emulsifying properties which may be of potential use in meat emulsion manufacturing
analysis
-
model for understanding the enormous rate enhancements affected by enzymes
analysis
-
popular system for protein engineering studies
analysis
-
analytical on-line liquid chromatography/bioassay with which both chemical and biological information on inhibitory effect of proteins in mixtures can be obtained simultaneously. Assay consists of protein separation using gel filtrationand subsequent homogeneous assay to distinct between active enzyme inhibitors and non-active compounds
analysis
-
due to high pI-value of enzyme, it does not migrate in the electrophoretic field in the Laemmli buffer system. Fast and simple identification of enzyme by over-running electrophoretic technique with a miniscale culture supernatant
analysis
-
due to high pI-value of enzyme, it does not migrate in the electrophoretic field in the Laemmli buffer system. Fast and simple identification of enzyme by over-running electrophoretic technique with a miniscale culture supernatant
analysis
-
due to high pI-value of enzyme, it does not migrate in the electrophoretic field in the Laemmli buffer system. Fast and simple identification of enzyme by over-running electrophoretic technique with a miniscale culture supernatant
-
biotechnology
-
subtilisin-30 kDa gamma-glutamyl transpeptidase complex exhibits better catalytic properties and can be exploited in various biotechnological applications
biotechnology
-
subtilisin-like serine protease has a great advantage over other proteases in high resistance to heat, denaturants, detergents and chelating agents and therefore has great potential for application in biotechnology fields
detergent
-
easy and flexible green fluorescence protein based assay for enzymic activity, which is performed under almost authentic washing conditions
detergent
-
formation of spherical dry granules with a diameter of 0.5 mm encapsulating active enzyme by emulsification of 2% alginate sol loaded with enzyme. Enzyme mass yields are about 50%, specific activity ranges from 60% to 100%, granules are appropriate for use in detergent application
detergent
enzyme SaP can be useful for industrial application operating over a broad temperature range, such as household detergent formulations
detergent
the enzyme subtilisin Carlsberg is industrially applied as an ingredient in various detergent products
detergent
-
the Fe protease has an excellent stain removal effect especially on blood and egg stains
detergent
-
enzyme SaP can be useful for industrial application operating over a broad temperature range, such as household detergent formulations
-
detergent
-
the Fe protease has an excellent stain removal effect especially on blood and egg stains
-
detergent
-
enzyme SaP can be useful for industrial application operating over a broad temperature range, such as household detergent formulations
-
industry
-
improving the kinetic, thermal and thermodynamic stability of subtilisin Carlsberg by means of simple, inexpensive but effective covalent coupling to oxidized sucrose polymers of varying sizes as well as polyglutaraldehyde. Stability is comparable to the most stabilized subtilisin variants obtained by site-directed mutagenesis
industry
subtilisin JB1 may serve as a potential source material for use in industrial applications of proteolytic enzymes and microorganisms for fishery waste degradation and fish by-product processing
industry
-
the enzyme shows excellent performance in stain removal from cotton fabric and good compatibility with several commercial laundry detergent formulations, suggesting that it has high potential for use in various industrial applications
industry
-
the enzyme shows excellent performance in stain removal from cotton fabric and good compatibility with several commercial laundry detergent formulations, suggesting that it has high potential for use in various industrial applications
-
industry
-
subtilisin JB1 may serve as a potential source material for use in industrial applications of proteolytic enzymes and microorganisms for fishery waste degradation and fish by-product processing
-
medicine
-
fibrinolytic activiy of strain DJ-4, develop the enzyme for its use as a thrombolytic agent
medicine
-
expression during non-fatal human rhinoorbital mucormycosis
medicine
-
fibrinolytic activiy of strain DJ-4, develop the enzyme for its use as a thrombolytic agent
-
synthesis
-
C221 subtilisin is catalytically wounded to the point that will barely hydrolyze peptide bonds but turn to be quite reactive with certain activated ester substrates, therefore a useful tool for catalyzing synthetic reactions
synthesis
-
subtilisin BPN' is an important industrial enzyme
synthesis
-
production of (R)-(2-methylpropyl)butanedioic acid 4-ethyl ester
synthesis
-
production of (R)-2-benzyl-3-[[1-methyl-1-((morpholin-4-yl)-carbonyl)ehtyl]sulfonyl]propionic acid-ethyl ester, which was prepared as an intermediate for the renin inhibitors ciprokiren and remikiren
synthesis
-
production of (S)-2-benzyl-3-(tert-butylsulfonyl)propionic acid, which was prepared as an intermediate for the renin inhibitor remikiren
synthesis
-
production of phenylalanine, which is used as an intermediate for the synthesis of aspartame
synthesis
-
conjugation of enzyme with comb-shaped poly-(ethylen glycol) and solubilization in ionic liquids without adding water. Enzyme exhibits higher transesterification activity in solution of [Eminm][Tf2N] than in toluene. No enzymic activity in DMSO, THF, or acetonitrile
synthesis
-
preparation of liposomes containing the enzyme and modulation of membrane permeability by cholate results in a nano-bioreactor system with higher apparent substrate selectivity than free enzyme due to different permeation of membrane by the substrates
synthesis
-
synthesis of benzyloxycarbonyl-L-Asp-L-Ser-NH2 with benzyloxycarbonyl-L-Asp methyl ester as acyl donor and serine amide as the nucleophile. Optimum conditions are pH 10.0, 35°C, in acetonitrile/Na2CO3-NaHCO3 buffer system, 85:15, with a dipeptide yield of 75.5%
synthesis
-
the engineered enzyme displays synthetically useful enantioselectivity for most of the secondary alcohols tested. The enantioselectivity of ISCBLS is in particular good to high for m- or p-substituted 1-phenylethanols. The dynamic kinetic resolutions of these secondary alcohols by the combination of ISCBLS and a ruthenium-based racemization catalyst provide the products of (S)-configuration with good results (80-94% yield, 90-99% enantiomeric excess). Enzyme CBLS is of great use as the enantiocomplementary counterpart of (R)-selective lipase for the dynamic kinetic resolution of secondary alcohols
synthesis
the enzyme subtilisin Carlsberg (SC) is industrially applied or synthetic organic chemistry applications, it has been used to enrich the S enantiomer of a racemic alcohol mixture by dynamic kinetic resolution (DKR) systems by combining SC with a ruthenium complex in organic solvent
additional information
-
ability of poly(ethylene)-glycol-modification to systematically modulate the structural dynamics of subtilisin Carlsberg in 1,4-dioxane. At increasing levels of modification the enzyme becomes more flexible, thus catalytically more active. In contrast, increasing the enzyme flexibility through poly(ethylene)-glycol-modification reduces the enzyme enantioselectivity
additional information
-
biocatalyst preparations which are capable of yielding higher/adequate transesterifaction activity of subtilisin in ionic liquids
additional information
-
Gly56 is required in stabilizing the propeptide fold. Stabilization of this fold leads to strong binding of the propeptide to subtilisin, high resistance of the propeptide to proteolytic degradation, and slow maturation of Pro-subtilisin
additional information
-
predicting protein interaction interfaces from sequences by using PAM matrix (PIFPAM) and subtilisin Carlsberg (1CSE chain E) as a reference sequence. The advantage of PIFPAM is that it is capable of predicting interaction interfaces from sequences without 3D structure information
additional information
-
slow folding of subtilisin results from the formation of an unstable and topologically challenged intermediate and the proline-limited isomerization of the intermediate to the native state
additional information
-
the subtilisin Karlsberg complex with sodium dodecyl sulfate in anhydrous organic solvents is an effective catalyst of peptide synthesis with multifunctional amino acids in positions P 1 and (Glu, Arg, and Asp) containing unprotected side ionogenic groups