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3.4.21.62: Subtilisin

This is an abbreviated version!
For detailed information about Subtilisin, go to the full flat file.

Word Map on EC 3.4.21.62

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.62 Subtilisin

Crystallization

Crystallization on EC 3.4.21.62 - Subtilisin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.4 A resolution
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structure of the processed protein is determined at 2.6 A resolution and compared with that of the full-length protein, in which the N-terminal extension binds back over the active site. A conserved proline introduces a backbone kink that shifts the scissile bond beyond reach of the catalytic serine and in addition the catalytic triad is disrupted. In the processed form, access to the active site is unblocked by removal of the N-terminal extension and the catalytic triad rearranges to a functional conformation
subtilisin Carlsberg covalently bound to the inhibitor L-[(1R)-1-acetamido-2-(1-naphthyl)ethyl]boronic acid, refined at 2.65 A is used in the studies
the structure is determined to a resolution of 1.56 A. ISP from Bacillus clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues
1.8 A resolution structure of an inactive form (by replacing the catalytic nucleophile Ser 221 with alanine) of the protease subtilisin S189, in complex with azide and with a prodomain substrate that spans the active site. The substrate is well ordered across the active site, and the azide anion is observed bound adjacent to Ala 32. Although S189, like wild-type subtilisin, has Ser as the catalytic nucleophile at residue 221, these crystal structures have Ala 221 to prevent cleavage of the substrate
in complex with chymotrypsin inhibitor 2 and its mutants M59K, M59Y, M59F, M59A, M59G, Y61A
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wild-type and thermostable mutant 7150 subtilisin at 1.8 A resolution
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by the batch method from buffer solution saturated with Na2SO4 ca. 13% (w/v) as precipitant. Placement of several Cs+ and Cl- ions in crystals of subtilisin Carlsberg. The protein conformation is very similar to that of the enzyme without CsCl in acetonitrile. 11 defined sites for Cs+ cations and 8 Cl- anions around the protein molecule, although most of these have partial occupancy and may represent nonspecific binding sites. Two Cs+ and two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis. CsCl-treated subtilisin crystals transferred to acetonitrile show catalytic activity several fold higher than the reference crystals containing Na+
subtilisin DY in a 1:1 complex with the synthetic inhibitor N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone, space group P2(1)2(1)2(1), unit cell dimensions of a = 5.28 nm, b = 7.27 nm and c = 5.98 nm
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trans-cinnamoyl-subtilisin, space group P2(1)2(1)2(1), unit cell dimensions in H2O a = 77.0, b = 55.0, c = 53.6, unit cell dimensions in acetonitrilea = 76.4 A, b = 55.3 A and c = 52.8 A
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crystal structure at 2.5 A
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crystal structure determined by molecular replacement, crystals grown in hanging drops, monoclinic space group P2(1), with cell dimensions a : 44.1 A, b : 51.7 A, c : 52.8 A, coordinates and structure factor amplitudes in the ProteinDataBank codes 1DBI and R1DBISF
crystal structure of a subtilisin BPN' complex with N-benzoyl-L-Arg
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crystal structure of subtilisin BPN' with Streptomyces subtilisin inhibitor at 2.6 A and 4.3 A
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crystal structure of subtilisin E with PMSF inhibitor at 2 A resolution
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crystallographic study
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refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c
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refined crystal structure of complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution
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refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins
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structure at 2.5 A resolution
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crystal structure of subtilisin E with PMSF inhibitor at 2 A resolution
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purified recombinant His-tagged enzyme, mixing of 30 mg/ml protein in 30 mM Tris-HCl, pH 7.4, and 150 mM NaCl, with 0.15 M ammonium sulfate, 15% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.0, X-ray diffraction structure determination and analysis at 1.83-1.90 A, molecular replacement and modeling
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subtilisin S41 surface is rich in hydrophilic residues, particularly Asp, which may contribute to its adaptation to psychrophilic conditions
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X-ray analysis
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by the hanging-drop vapour-diffusion method. Crystals of AprB2 diffract to 1.7 A resolution. The crystals belong to space group P1, with unit-cell parameters a = 42.7, b = 45.8, c = 45.7 A , alpha = 98.4, beta = 114.0, gamma = 114.6. The crystals contain one molecule in the asymmetric unit, with a solvent content of 36%
by the hanging-drop vapour-diffusion method. Crystals of AprV2 diffract to 2.0 A resolution. The crystals belong to space group P1, with unit-cell parameters a = 43.1, b = 46.0, c = 47.2 A , alpha = 97.8, beta = 115.2, gamma = 115.2. The crystals contain one molecule in the asymmetric unit, with a solvent content of ca. 36%
by the hanging-drop vapour-diffusion method. Crystals of BprB diffract to 1.8 A resolution. The crystals belong to space group P21, with unit-cell parameters a = 38.5, b = 90.5, c = 44.1 A , beta = 109.9. The crystals contain one molecule in the asymmetric unit, with a solvent content of 36%
by the hanging-drop vapour-diffusion method. Crystals of BprV diffract to 2.0 A resolution. The crystals belong to space group P21, with unit-cell parameters a = 38.5, b = 89.6, c = 47.7 A , beta = 113.6. The crystals contain one molecule in the asymmetric unit, with a solvent content of 40%
crystal structure shows that an unusual extended disulfhide-tethered loop functions as an exosite, mediating effective enzyme-substrate interactions. The disulphide bond and Tyr92, which is located at the exposed end of the loop, is functionally important
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data reveal that that the S1 pocket of BprB is less hydrophobic but bigger than that of basic protease BprV (sequence homologue)
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data reveal that that the S1 pocket of BprV is more hydrophobic but smaller than that of basic protease BprB
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at 1.4 A resolution
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crystal structure at 1.4 A resolution
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hanging drop vapor diffusion, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of 52.65 A, 61.25 A and 74.75 A
by the hanging drop vapor-diffusion method, at 0.8 A resolution. Crystals belong to the monoclinic space group P21. Unit cell parameters are a = 46.09 A, b = 62.67 A, c = 84.87 A, and beta = 95.5°, indicating two molecules of Sph in the asymmetric unit. The crystal structures of the psychrophilic Bacillus TA41 subtilisin S41 and the mesophilic subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule
by the hanging drop vapor-diffusion method, at 1.4 A resolution. Crystals belong to either the tetragonal space group P41212 or P43212. Unit cell dimensions are a = b = 61 A and c = 174.77 A , indicating one monomer in the asymmetric unit. The crystal structures of the psychrophilic subtilisin S41 and the mesophilic Bacillus sphaericus subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule
serine protease inhibitor CrSPI-1 complexed with subtilisin. Crystals diffracted to 2.6 A resolution and belong to space group P2(1), with unit-cell parameters a = 73.8, b = 65.0, c = 111.9 A, beta = 95.4. Presence of one heterotrimer (1:2 ratio of CrSPI-1:subtilisin) and one free subtilisin molecule in the asymmetric unit
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a comparative study of psychrophilic, mesophilic and thermophilic subtilisin-like serine proteases by all-atom molecular dynamics simulations is performed. The thermophilic subtilisin presents a high affinity calcium binding site which is not structurally conserved in the mesophilic and psychrophilic counterparts, which at the same position show a stable salt bridge network and no stabilizing intra-molecular interactions, respectively
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by sitting-drop, vapor-diffusion method. Crystal structures of the autoprocessed/unautoprocessed form and mature forms of subtilisin at 1.89 A and 1.70 A resolution, respectively. Crystals show a unique Ca2+-binding site and that the N-terminal region of the mature domain (Gly70–Pro82), which binds tightly to the main body in the unautoprocessed form, is disordered and mostly truncated in the autoprocessed and mature forms, respectively. Crystal structure of the propeptide:S324A-subtilisin complex at 1.65 a resolution
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by the sitting drop vapor diffusion method. Crystal structures of propeptides in complex with S324A-subtilisin. Conformation of the propeptide is altered by the mutation, such that nonglycine residues at position 56 assume a right-handed conformation and hydrophobic interactions at the core region decrease
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pro-S255A crystallized in complex with Ca2+, by sitting-drop vapour-diffusion method, to 2.3 A resolution. Crystal belongs to space group I222, with unit cell parameters a = 92.69, b = 121.78, c = 77.53 A. Matthews coefficient is 2.6 A 3 Da-1 and the solvent content is 53.1%.
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high content of acidic residues mainly found on its surface, making it charged