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.
H186T
-
no effect on enzyme specificity, 4.9fold increase in KM-value, 600fold decrease in kcat-value
DELTA1-48
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-55
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-60
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-62
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-64
-
poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, very low activity
DELTA1-65
-
poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, activity hardly detectable
E62Q/E65S
-
mutation prevent degradation of protein, slightly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
E62Q/E65S/A67P/N68P
-
efficient suppression of proteolysis, strongly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
G176E/Q179E/Y185W/D189P/K191E/Y192F/S194G/S195A
-
GluV8DELTAC, the C-terminal 52 residues are deleted
S237A
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, no proteinolytic activity
S66R
-
insertion of a trypsin degradable sequence, successful enzyme processing by trypsin instead of thermolysin, enhanced Glu-specific activity
V69A
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
V69F
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
V69G
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
K191E/Y192F/S194G/S195A
-
GluSE-EFGA
N190H/Y192H/S169A
-
the specific activity of the mutant is 4.5fold increased from that of the wild type enzyme. The mutant potently hydrolyzes LLE-7-amido-4-methylcomarin
S66R/V69A
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 4.5% of activity compared with the Val69 native form
S66R/V69F
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.4% of activity compared with the Val69 native form
S66R/V69G
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.1% of activity compared with the Val69 native form
S66R/V69S
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 0.6% of activity compared with the Val69 native form
Y185W/D189P
-
the activity of GluSE with the two substitutions, i.e., Y185W and D189P (designated GluSE-WP), is equivalent to that of GluSE-WPEFGA
Y185W/D189P/K191E/Y192F/S194G/S195A
-
GluSE/WPEFGA
N190H/Y192H/S169A
-
the specific activity of the mutant is 4.5fold increased from that of the wild type enzyme. The mutant potently hydrolyzes LLE-7-amido-4-methylcomarin
-
H199V
-
change in the substrate preference, with a 16fold increase in the ratio of turnover number to Km-value with substrates with Phe in P1, and a 20fold increase with substrates with Glu in P1. Substitution of His199 by anything except Val completely abolishes the production of mature enzyme
H228A
-
change in substrate specificity, i.e., a slight increase in the ratio of turnover-number to Km-value for the substrate with Asp and a more than 300-fold increase in this ratio when P1 substituent is Ala
S216A
-
about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme
S216G
-
about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme
S168C
-
the mutant does not show proteolytic and azocaseinolytic activity
additional information
-
mutations within the amino acid sequence alpha17-40 influence the organic co-solvent-induced conformation and concomittant resistance of E30-R31 peptide bond to cleavage occurs, alteration of the thermaldynamic stability of the splicedon, the flanking regions are involved in stabilization
additional information
-
mature protein sequence is fused with the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, suppression of protein degradation, accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
additional information
-
chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B
additional information
-
GluV8mut5, full-length GluV8 with five substitutions (Asp36His/Glu62Gln/Glu65Ser/Ala67Pro/Asn68Ser) in the prosegment, GluV8mut5DELTAC, GluV8mut5 with C-terminal 52 residues deleted, GluV8mut4nCSer237Ala, GluV8mut4nC with an amino acid substitution (Ser237Ala), GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
additional information
-
GluV8mut5, full-length GluV8 with five substitutions (Asp36His/Glu62Gln/Glu65Ser/Ala67Pro/Asn68Ser) in the prosegment, GluV8mut5DELTAC, GluV8mut5 with C-terminal 52 residues deleted, GluV8mut4nCSer237Ala, GluV8mut4nC with an amino acid substitution (Ser237Ala), GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
-
additional information
-
chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B. GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW
additional information
-
GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW
additional information
-
GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
additional information
-
GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
-