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evolution
Q0WWH7
phylogenetic analysis, AtSASP and its putative orthologues clustering in one discrete group of subtilisin proteases in which no other Arabidospsis subtilisin protease is present. The enzyme function is at least partially conserved between Arabidopsis thaliana and Oryza sativa
evolution
the enzyme belongs to a structurally distinct class of the subtilase family
evolution
the enzyme is a member of the peptidases_S8/PCSK9/proteinase K-like family (Pf00082)
evolution
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the subtilisin-like proteases share the same catalytic mechanism as the trypsin-like proteases, depending upon the hydroxyl group of a serine residue. The catalytic triad of subtilisin-like proteases is composed of Asp, His, and Ser. Due to its different specificity compared to the members of the S8 family of clan SB of proteases, the Fe protease might be a protease distinct from previously defined IUBMB groups of proteases, it is no member of the the S8 peptidase family
evolution
enzyme SOPT has a PEXEL-like sequence, is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and is orthologous to Plasmodium falciparum SOPT. The function of SOPT is conserved in different Plasmodium species, overview
evolution
enzyme SOPT has a PEXEL-like sequence, it is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and it is orthologous to Plasmodium berghei PIMMS2. The function of SOPT is conserved in different Plasmodium species, overview
evolution
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enzyme subtilisin E-S7 (SES7) has 3 amino acids different from subtilisin E (1SCJ): S85A, T130S, and T162S
evolution
IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
evolution
subtilisin QK is highly homologous to nattokinase (NK, Q548F3)
evolution
the Arabidopsis thaliana genome encodes 56 subtilisin-like serine proteases (subtilases), enzyme AtSBT1.9 is a member of the subtilase subfamily 1
evolution
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the enzyme belongs to the S8 peptidase family
evolution
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enzyme SOPT has a PEXEL-like sequence, is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and is orthologous to Plasmodium falciparum SOPT. The function of SOPT is conserved in different Plasmodium species, overview
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evolution
Vibrio cholerae serotype O1 C6706
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IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
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evolution
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the subtilisin-like proteases share the same catalytic mechanism as the trypsin-like proteases, depending upon the hydroxyl group of a serine residue. The catalytic triad of subtilisin-like proteases is composed of Asp, His, and Ser. Due to its different specificity compared to the members of the S8 family of clan SB of proteases, the Fe protease might be a protease distinct from previously defined IUBMB groups of proteases, it is no member of the the S8 peptidase family
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evolution
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the enzyme is a member of the peptidases_S8/PCSK9/proteinase K-like family (Pf00082)
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evolution
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the Arabidopsis thaliana genome encodes 56 subtilisin-like serine proteases (subtilases), enzyme AtSBT1.9 is a member of the subtilase subfamily 1
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evolution
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subtilisin QK is highly homologous to nattokinase (NK, Q548F3)
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evolution
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IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
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evolution
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the enzyme belongs to the S8 peptidase family
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evolution
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enzyme subtilisin E-S7 (SES7) has 3 amino acids different from subtilisin E (1SCJ): S85A, T130S, and T162S
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evolution
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IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
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malfunction
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gene knock-out results in reduced ability by the parasite to undergo promastigote to amastigote differentiation in vitro. SUB-deficient Leishmania display reduced virulence in infection models. SUB knock-out parasites show altered regulation of the terminal peroxidases of the trypanothione reductase system and the predominant tryparedoxin peroxidases are decreased in SUB-/- parasites. knock-out parasites show increased sensitivity to hydroperoxide. Data suggest that subtilisin is the maturase for tryparedoxin peroxidases and is necessary for full virulence
malfunction
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using a protease mutant of Dichelobacter nodosus it is shown in a sheep virulence model that AprV2 is required for virulence
malfunction
Q0WWH7
at maturity, enzyme knockout sasp-1 plants produce 25% more inflorescence branches and siliques, mostly due to an increased number of second and third order branches, than either the wild-type or the rescued lines
malfunction
SOPT-deficient parasites develop normally through the asexual and sexual stages and produce equivalent numbers of ookinetes to NF54 controls, but they form fewer oocysts and sporozoites in mosquitoes
malfunction
the mutant PbDELTASOPT/PIMMS2 produces low numbers of salivary gland sporozoites
malfunction
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the mutant PbDELTASOPT/PIMMS2 produces low numbers of salivary gland sporozoites
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physiological function
AcpII comprises a prepropeptide, a catalytic domain that includes a protease-associated domain, and tandem repeat prepeptidase C-terminal domains
physiological function
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alcalase-hydrolyzed potato protein has both antioxidant and emulsifying properties
physiological function
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during growth of Pichia pastoris, Sub2 is produced as a secreted enzyme at a concentration of 10 microg/ml of culture supernatant after overexpression of the full-length SUB2 gene. During fermentative production of recombinant enzymes in methanol medium, 1 ml of Pichia pastoris culture supernatant is found to contain approximately 3 ng of Sub2, while the enzyme is not detected during growth in a medium containing glycerol as a carbon source
physiological function
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is involved in Streptococcus suis virulence
physiological function
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isolation of angiotensin I-converting enzyme inhibitory peptide from hydrolysates and enzymatic digests of Spirulina platensis by alcalase. The digests by alcalase with a molecular weight range of 0-3000 show the most potent inhibitory activity of 0.23 mg/ml with a yield of 15.0% among tested hydrolysates
physiological function
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peanut hydrolysate obtained after 6 h of digestion by alcalase used to isolate angiotensin I converting enzyme inhibitory peptides
physiological function
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Pro-subtilisin-like serine protease consists of an N-terminal propeptide (Ala1-Ala113), a mature domain (subtilisin-like serine protease, Val114-Val539) and a C-terminal propeptide (Asp540-Gly640)
physiological function
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significantly inhibits carrageenan-induced mouse tail thrombus formation in vivo. Inhibition activity increases along with the injection amount of subtilisin QK, which presents linearity relationship. When the amount of subtilisin QK reaches 12000 IU, thrombus nearly disappears in mouse tail
physiological function
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silk fibroin hydrolysate obtained through alcalase digestion demonstrates in vitro angiotensin I converting enzyme inhibitory activity and in vivo antihypertensive activity in spontaneously hypertensive rats. Degrees of hydrolysis and angiotensin I converting enzyme inhibitory activities is related with hydrolysis period of silk fibroin hydrolysates obtained with alcalase treatments: highest angiotensin I converting enzyme inhibitory activities (72.5%) are obtained with a hydrolysis time of 105 min, whereby degree of hydrolysis is 17.1%
physiological function
strains causing benign footrot secrete AprB2
physiological function
strains causing benign footrot secrete subtilisin-like protease BprB
physiological function
strains causing virulent footrot secrete the subtilisin-like protease AprV2
physiological function
strains causing virulent footrot secrete the subtilisin-like protease BprV
physiological function
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subtilisin enhances transpeptidase activity of 67 kDa gamma-glutamyl transpeptidase and 30 kDa gamma-glutamyl transpeptidase, by nearly 1.5- and 2fold, respectively. In presence of subtilisin, 30 kDa gamma-glutamyl transpeptidase has improved catalytic efficiency, altered pH and temperature optima and has salt-tolerant glutaminase activity
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
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when subtilisin C. is chemically modified with polyethylene glycol and inhibited with a dansyl fluorophore, and initially dissolved in two organic solvents (acetonitrile and 1,4-dioxane), the active site environment of the enzyme is similar to that in water. Prolonged exposure to the organic medium causes this environment to resemble that of the solvent in which the enzyme is dissolved
physiological function
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acts extracellularly in the apoplast of stomatal precursor cells where it may be involved in the generation of signals responsible for stomata density regulation
physiological function
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enzyme shows caspase specificity
physiological function
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enzyme shows caspase specificity
physiological function
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implicated in fragmentation of the membrane-bound transcription factor AtbZIP1723 and precursors of pectin methylesterase and rapid alkalinization growth factor
physiological function
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involved in proteolysis of the seed storage protein, beta-conglycinin
physiological function
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pathogenesis related protein which is shown to be one of several subtilases that are specifically induced following pathogen infection. P69 is suggested to process a leucin-rich repeat cell wall protein in virus-infected tomato plants
physiological function
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principal allergen produced by Aspergillus strains
physiological function
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some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. Enzyme is implicated the proteolytic degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) during biotic and abiotic programmed cell death
physiological function
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some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. In response to death-inducing stimuli, phytaspase is shown to re-localize to the cell interior
physiological function
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some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. In response to death-inducing stimuli, phytaspase is shown to re-localize to the cell interior
physiological function
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Subtilisin A applied at nanomolar concentrations suppresses epileptiform spikes in rat hippocampal slices and neocortex in vivo
physiological function
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the subtilase ALE1 is involved in the generation of peptide signals that are required for cuticle formation and epidermal differentiation during Arabidopsis embryo development
physiological function
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a cold-adapted protease, residue Ala284 is an important cold-adaptation determinant of the enzyme
physiological function
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fungal subtilisin is a defense elicitor, culture filtrates from avirulent Acremonium spp. induce resistance against pathogens in strawberry plants or accumulation of reactive oxygen species (e.g. H2O2 and O2 -) and callose in Arabidopsis thaliana plants, expression analysis of defense-related genes in strawberry and defense responses induced by the enzyme in Arabidopsis leaves, overview
physiological function
modeling of intracellular subtilisin protease regulation within the cell
physiological function
Q0WWH7
the enzyme downregulates branching and silique production during monocarpic senescence
physiological function
the serine protease may be involved in both mycoparasitism and antibiotic secretion
physiological function
Plasmodium berghei PbSOPT/PIMMS2 is dispensable for ookinete development, and PbSOPT/PIMMS2 is dispensable for sporozoite infectivity and establishing patency. PIMMS2 is involved in midgut traversal in Anopheles gambiae. SOPT facilitates transmission of Plasmodium berghei ookinetes to mosquitoes
physiological function
Plasmodium falciparum subtilisin-like ookinete protein SOPT plays an important and conserved role during ookinete infection of the Anopheles stephensi midgut. It may be involved in infecting the human or mosquito host. SOPT facilitates transmission of Plasmodium falciparum ookinetes to mosquitoes
physiological function
subtilisin Carlsberg is a serine protease naturally secreted from Bacillus licheniformis
physiological function
Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
physiological function
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Plasmodium berghei PbSOPT/PIMMS2 is dispensable for ookinete development, and PbSOPT/PIMMS2 is dispensable for sporozoite infectivity and establishing patency. PIMMS2 is involved in midgut traversal in Anopheles gambiae. SOPT facilitates transmission of Plasmodium berghei ookinetes to mosquitoes
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physiological function
Vibrio cholerae serotype O1 C6706
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Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
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physiological function
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the serine protease may be involved in both mycoparasitism and antibiotic secretion
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physiological function
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significantly inhibits carrageenan-induced mouse tail thrombus formation in vivo. Inhibition activity increases along with the injection amount of subtilisin QK, which presents linearity relationship. When the amount of subtilisin QK reaches 12000 IU, thrombus nearly disappears in mouse tail
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physiological function
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Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
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physiological function
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AcpII comprises a prepropeptide, a catalytic domain that includes a protease-associated domain, and tandem repeat prepeptidase C-terminal domains
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physiological function
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strains causing benign footrot secrete subtilisin-like protease BprB
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physiological function
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is involved in Streptococcus suis virulence
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physiological function
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Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
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physiological function
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strains causing virulent footrot secrete the subtilisin-like protease BprV
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physiological function
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strains causing virulent footrot secrete the subtilisin-like protease AprV2
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additional information
molecular modeling and docking analysis using crystal structure PDB ID 1yu6
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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structure homology modeling, structure comparisons, overview
additional information
structure molecular modeling using the crystal structure of the pro-subtilisin E complex, PDB ID 1SCJ, the active site Cys221 is replaced with the catalytic serine, molecular dynamics simulation, overview
additional information
substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets
additional information
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substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets
additional information
the catalytic triad residues consists of Ser221, Pro210 to His64
additional information
homology modeling of Plasmodium berghei SOPT, overview
additional information
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homology modeling of Plasmodium berghei SOPT, overview
additional information
homology modeling of Plasmodium falciparum SOPT, overview
additional information
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homology modeling of Plasmodium falciparum SOPT, overview
additional information
initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
additional information
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the Fe protease contains an insertion (amino acids 168-173 of the mature sequence) which is not present in the proteinase K sequence
additional information
the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
additional information
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the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
additional information
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homology modeling of Plasmodium berghei SOPT, overview
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additional information
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the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
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additional information
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initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
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additional information
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the Fe protease contains an insertion (amino acids 168-173 of the mature sequence) which is not present in the proteinase K sequence
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additional information
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initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
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