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3.4.21.19: glutamyl endopeptidase

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

Word Map on EC 3.4.21.19

Reaction

Preferential cleavage: Glu-/-, Asp-/- =

Synonyms

Alcalase, BIEP, BIGEP, BL-GSE, BLase, BS-GSE, endoproteinase Glu-C, endoproteinase V8, Glu C, Glu-C, Glu-endopeptidase, Glu-specific endopeptidase, GluScoh, GluScpr, GluSE, GluSsap, GluSW, glutamate specific endopeptidase, glutamate-specific proteinase, glutamate-specific serine endopeptidase, glutamic acid-specific endopeptidase, glutamic acid-specific proteinase, glutamic-acid-specific endopeptidase, glutamyl endopeptidase, glutamyl endopeptidase 2, glutamyl endopeptidase I, glutamyl specific endopeptidase, GluV8, GSE, gseBi gene product, protease V8, proteinase, glutamate-specific, proteinase, staphylococcal serine, SG-GSE, SGPE, Sspa, staphylococcal serine proteinase, V8 protease, V8 proteinase, V8-GSE, V8-protease, VSPase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.19 glutamyl endopeptidase

Engineering

Engineering on EC 3.4.21.19 - glutamyl endopeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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