Information on EC 3.4.24.28 - bacillolysin

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The expected taxonomic range for this enzyme is: Firmicutes

EC NUMBER
COMMENTARY
3.4.24.28
-
RECOMMENDED NAME
GeneOntology No.
bacillolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
similar, but not identical, to that of thermolysin
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Anilozyme P 10
-
-
-
-
Bacillus metalloendopeptidase
-
-
-
-
Bacillus metalloproteinase
-
-
-
-
Bacillus neutral proteinase
-
-
-
-
Bacillus polymyxa protease
-
-
Bacillus subtilis neutral proteinase
-
-
-
-
BL-MA
Bacillus megaterium A9542
-
-
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C histolyticum neutral protease
-
-
EC 3.4.24.4
-
-
formerly
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MCP 76
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-
-
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Megateriopeptidase
-
-
-
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MprBi
B3V4Z0
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Neutral protease
-
-
-
-
Neutral protease
-
-
Neutral protease
-
-
Neutral protease
-
-
non-specific neutral protease
-
-
Thermostable neutral protease
-
-
-
-
thermoysin-like proteinase
-
-
CAS REGISTRY NUMBER
COMMENTARY
76774-43-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene mprBi
UniProt
Manually annotated by BRENDA team
Bacillus megaterium A9542
A9542
-
-
Manually annotated by BRENDA team
strain 76
-
-
Manually annotated by BRENDA team
Bacillus pumilus 76
strain 76
-
-
Manually annotated by BRENDA team
var. amylosacchariticus
-
-
Manually annotated by BRENDA team
NCIB 8924 and NRRL B-3880
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
B3V4Z0, -
MprBi is a metzincin clan adamalysin/reprolysin-like metalloprotease and belongs to the class of zinc-dependent metalloproteinases
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CoCl2
-
0.3 mM, 1.8fold increase in activity
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0057
-
B3V4Z0, -
with substrate Dnp-AAVR, pH 8.0, 37C
0.0145
-
B3V4Z0, -
with substrate Dnp-GGLR, pH 8.0, 37C
0.0264
-
B3V4Z0, -
with substrate Dnp-GGK, pH 8.0, 37C
0.0282
-
B3V4Z0, -
with substrate Dnp-GGIR, pH 8.0, 37C
0.0365
-
B3V4Z0, -
with substrate Dnp-GGFR, pH 8.0, 37C
0.0515
-
B3V4Z0, -
with substrate Dnp-AALR-NH2, pH 8.0, 37C
17.4
-
B3V4Z0, -
with substrate azocasein, recombinant purified wild-type enzyme, pH 8.0, 37C
55.6
-
-
pH 6.5, 55C
78.5
-
-
Boilysin at 37C with casein as substrate
81.5
-
-
pseudo wild type at 37C with casein as substrate
81.9
-
-
wild type enzyme at 37C with casein as substrate
82.4
-
-
double mutant G8C/N60C at 37C with casein as substrate
242
-
-
wild type enzyme at temperature optimum 75C
273
-
-
pseudo wild type at temperature optimum 75C
375
-
-
double mutant G8C/N60C at temperature optimum 80C
608
-
-
boilysin at temperature optimum 95C
additional information
-
-
-
additional information
-
-
-
additional information
-
P43133
16530 microg Tyr produced per min, pH 7.5, 65C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
P43133
sharp decrease in activity below
6.5
11
-
decrease of activity from pH 6.5 to 11
11
-
-
no residual activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
B3V4Z0, -
assay at
60
-
-
activity toward N-(3-[2-furyl]acryloyl)-Gly-Leu amide is 4 times higher than at 25C
75
-
-
pseudo wild type; wild type enzyme
80
-
-
double mutant G8C/N60C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
70
B3V4Z0, -
activity range
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
B3V4Z0, -
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
B3V4Z0, -
secreted zinc-dependent endopeptidase
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE
?
-
x * 35300, SDS-PAGE
?
P43133
x * 35000, SDS-PAGE
?
B3V4Z0, -
x * 19000, SDS-PAGE
?
Bacillus megaterium A9542
-
x * 35300, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure at 3.0 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
1h, less than 40% remaining activity
4
-
-
60 min, complete loss of activity
5
8
-
stable within this range
5
9
-
37C, 60 min, stable
11.7
-
-
60 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ca2+ stabilizes against thermal inactivation
-
MgCl2 stabilizes
-
native wild type and G8C/N60C enzymes are stable toward autoproteolysis and keep their structural integrity for several weeks
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-propanol
-
48 h, 37C, 50% residual activity with 44.5% (v/v) and 65.5% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
Acetone
-
48 h, 37C, 50% residual activity with 30.0% (v/v) and 50.1% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
acetonitrile
-
48 h, 37C, 50% residual activity with 30.6% (v/v) and 51.6% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
dimethylformamide
-
48 h, 37C, 50% residual activity with 29.8% (v/v) and 45.8% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
dioxane
-
48 h, 37C, 50% residual activity with 32.1% (v/v) and 47.9% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
DMSO
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48 h, 37C, 50% residual activity with 32.9% (v/v) and 48.7% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
Methanol
-
48 h, 37C, 50% residual activity with 56.6% (v/v) and 86.4% (v/v) for pseudo wild-type and mutant G8C/N60C respectively
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protease activity can be significantly regained if the completely unfolded enzyme is transferred from 8 M guanidine-HCl into native-like conditions (0.4 M guanidine-HCl) by dilution with buffer
-
renaturation of enzyme from inclusion bodies after solubilization using guanidine hydrochloride
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
production of enzyme as an active mature enzyme in Escherichia coli in the absence of its prosequence. Expression of enzyme with N-terminal His-tag, which accumulates as inclusion bodies and renaturation after solubilization using guanidine hydrochloride