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
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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
Posttranslational Modification
Posttranslational Modification on EC 3.4.21.62 - Subtilisin
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proteolytic modification
prosequence regulates ISP activity through two distinct modes: active site blocking and catalytic triad rearrangement. The full-length proenzyme is inactive until specific proteolytic processing removes the first 18 amino acids that comprise the N-terminal extension, with processing appearing to be performed by ISP itself
proteolytic modification
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expressed as pre-pro-proteins whose prodomains are autocatalytically processed
proteolytic modification
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propeptide is absolutely required to fold into a kinetically trapped conformer. Comparison of folding kinetics and intermediates with intracellular serine proteases
proteolytic modification
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the enzyme propeptide is cleaved to the mature form
proteolytic modification
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the enzyme propeptide is cleaved to the mature form
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proteolytic modification
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sites of primary autoproteolysis of the purified recombinant Fe protease are Leu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease)
proteolytic modification
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sites of primary autoproteolysis of the purified recombinant Fe protease areLeu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease)
proteolytic modification
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autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease
proteolytic modification
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autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease
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proteolytic modification
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sites of primary autoproteolysis of the purified recombinant Fe protease are Leu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease)
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proteolytic modification
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sites of primary autoproteolysis of the purified recombinant Fe protease areLeu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease)
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proteolytic modification
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expressed as pre-pro-proteins whose prodomains are autocatalytically processed
proteolytic modification
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expressed as pre-pro-proteins whose prodomains are autocatalytically processed
proteolytic modification
the enzyme matures from the inactive precursor, Pro-Tk-subtilisin (Pro-TKS), upon autoprocessing and degradation of the propeptide (Tkpro)
proteolytic modification
in silico analyses predicts signal and pro-peptides at the N-terminus
proteolytic modification
IvaP undergoes extensive post-translational processing. Following secretion, enzyme IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, extracellular maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which can temporarily inhibit, and be cleaved by, the purified enzyme. IvaP processing results in the loss of about 139 amino acids (about 15 kDa) from the IvaP N-terminus and about 23 amino acids (about 3 kDa) from the IvaP C-terminus, cleavage pattern overview. These sequencing results are consistent with N-terminal cleavage of the 44-kDa IvaP intermediate to the fully cleaved 38-kDa form. A trypsin-like serine protease can cleave the inactive form of IvaP. IvaP exhibits strain-specific processing, comparisons of strains C6706, Haiti, E7946, and N1696
proteolytic modification
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IvaP undergoes extensive post-translational processing. Following secretion, enzyme IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, extracellular maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which can temporarily inhibit, and be cleaved by, the purified enzyme. IvaP processing results in the loss of about 139 amino acids (about 15 kDa) from the IvaP N-terminus and about 23 amino acids (about 3 kDa) from the IvaP C-terminus, cleavage pattern overview. These sequencing results are consistent with N-terminal cleavage of the 44-kDa IvaP intermediate to the fully cleaved 38-kDa form. A trypsin-like serine protease can cleave the inactive form of IvaP. IvaP exhibits strain-specific processing, comparisons of strains C6706, Haiti, E7946, and N1696
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proteolytic modification
Vibrio cholerae serotype O1 C6706
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IvaP undergoes extensive post-translational processing. Following secretion, enzyme IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, extracellular maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which can temporarily inhibit, and be cleaved by, the purified enzyme. IvaP processing results in the loss of about 139 amino acids (about 15 kDa) from the IvaP N-terminus and about 23 amino acids (about 3 kDa) from the IvaP C-terminus, cleavage pattern overview. These sequencing results are consistent with N-terminal cleavage of the 44-kDa IvaP intermediate to the fully cleaved 38-kDa form. A trypsin-like serine protease can cleave the inactive form of IvaP. IvaP exhibits strain-specific processing, comparisons of strains C6706, Haiti, E7946, and N1696
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proteolytic modification
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IvaP undergoes extensive post-translational processing. Following secretion, enzyme IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, extracellular maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which can temporarily inhibit, and be cleaved by, the purified enzyme. IvaP processing results in the loss of about 139 amino acids (about 15 kDa) from the IvaP N-terminus and about 23 amino acids (about 3 kDa) from the IvaP C-terminus, cleavage pattern overview. These sequencing results are consistent with N-terminal cleavage of the 44-kDa IvaP intermediate to the fully cleaved 38-kDa form. A trypsin-like serine protease can cleave the inactive form of IvaP. IvaP exhibits strain-specific processing, comparisons of strains C6706, Haiti, E7946, and N1696
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additional information
Q0WWH7
occurrence of the two variant forms of AtSASP can be due to posttranslational modifications
additional information
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occurrence of the two variant forms of AtSASP can be due to posttranslational modifications
additional information
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contains no carbohydrate
additional information
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contains no carbohydrate
additional information
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contains no carbohydrate