Information on EC 3.4.24.29 - aureolysin

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The expected taxonomic range for this enzyme is: Staphylococcus aureus

EC NUMBER
COMMENTARY hide
3.4.24.29
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RECOMMENDED NAME
GeneOntology No.
aureolysin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
39335-13-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A152
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Manually annotated by BRENDA team
a clinical isolate
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Manually annotated by BRENDA team
strain RN4220
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Manually annotated by BRENDA team
strain V8
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Manually annotated by BRENDA team
strain V8-BC 10
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the sigB mutant strain overexpresses the surface-anchored protein Bap, that is essential for biofilm formation in the model strain. Staphylococcus aureus completely inhibits the biofilm formation of the mutant strain via Aur and SspA, two proteases that are overexpressed in the sigB mutant strain and are capable of degrading Bap
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-toxin + H2O
?
show the reaction diagram
alpha2-macroglobulin + H2O
?
show the reaction diagram
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processing of the inhibitor, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
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?
Bap + H2O
?
show the reaction diagram
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a surface-anchored protein
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-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
cathelicidin LL-37 + H2O
?
show the reaction diagram
complement component C3 + H2O
C3a+SN + C3b2SN
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
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-
-
-
?
GWTLNSAGYLLGPHAIDNHRSFHDKYGLA-NH2 + H2O
Gly-Trp-Thr + Leu-Asn-Ser + Ala-Gly + Tyr + Leu + LGPHAIDNHRS + FHDKYG + Leu-Ala-NH2
show the reaction diagram
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i.e. galanin
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?
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
Nalpha-furylacryloyl-Gly-Ala-NH2 + H2O
?
show the reaction diagram
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very poor substrate
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?
Nalpha-Furylacryloyl-Gly-Leu amide + H2O
?
show the reaction diagram
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Nalpha-furylacryloyl-Gly-Leu-NH2
?
show the reaction diagram
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Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
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?
Nalpha-furylacryloyl-Gly-Phe-NH2
?
show the reaction diagram
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Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
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?
Nalpha-furylacryloyl-Gly-Val-NH2 + H2O
?
show the reaction diagram
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very poor substrate
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?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
show the reaction diagram
plasminogen + H2O
angiostatin + mini-plasminogen
show the reaction diagram
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?
plasminogen activator inhibitor-1 + H2O
?
show the reaction diagram
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processing of the inhibitor, the proteolytic degradation of PAI-1 by aureolysin is associated with a drastic decrease in its capacity to inhibit uPA, down to 7% of the inhibitory activity of the control PAI-1
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?
pro-urokinase-type plasmin activator + H2O
2 chains of urokinase-type plasmin activator
show the reaction diagram
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human substrate, activation by cleavage into two enzyme chains, activity by wild-type strains 8325-4 and Newman, and clinical isolates, overview, no activity with N-terminal enzyme substrate mutants, overview
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?
SspA zymogen + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bap + H2O
?
show the reaction diagram
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a surface-anchored protein
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-
?
cathelicidin LL-37 + H2O
?
show the reaction diagram
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human antimicrobial peptide. Enzyme production by Staphylococcus aureus contributes to its resistance to the innate immune system of humans mediated by LL-37
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?
complement component C3 + H2O
C3a+SN + C3b2SN
show the reaction diagram
SspA zymogen + H2O
?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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slight stimulation of protease I
Pb2+
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slight stimulation of protease I
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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Ag2+
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protease II
alpha2-Macroglobulin
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a regulatory serpin, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
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Co2+
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protease II inactive in presence of, protease I slightly stimulated
Cu2+
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protease II
DFP
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1.0 mM, 30 min, 20°C, activity of protease I is reduced by 10%, activity of protease II by 30%
Hg2+
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protease II
Mn2+
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protease II
NaCl
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50% reduction of activity at 0.3 M for protease I and 0.5 M for protease II
plasminogen activator inhibitor-1
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PAI-1, a regulatory serpin, interaction analysis with aureolysin, overview, the proteolytic degradation of PAI-1 by aureolysin is associated with a drastic decrease in its capacity to inhibit uPA, down to 7% of the inhibitory activity of the control PAI-1
Zn2+
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protease II
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Reducing agents
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protease II active only in presence of reducing agents such as cysteine, 2-mercaptoethanol or sodium thioglycollate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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and 7.0-9.0, hemoglobin, protease I
7 - 9
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and 5.0, hemoglobin, protease I
7.4 - 7.8
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assay at
7.8
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casein, protease I
8.8
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casein, protease II
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12500
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Staphylococcus aureus, protease II, gel filtration
21000
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Staphylococcus aureus, protease I, gel filtration
26800
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Staphylococcus aureus, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 38000, Staphylococcus aureus, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inhibitor-free form, cristall from sitting-drop vapour-diffusion method, refinement by molecular replacement
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
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37°C, 3 h, protease I stable
31167
7
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37°C, 3 h, 47% loss of activity, protease II
31167
8
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37°C, 3 h, 74% loss of activity, protease II
31167
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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pH 4.0-11.0, 3 h, protease I stable
45
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pH 7.0, 30 min, stable up to, protease I
50
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pH 7.0, 30 min, 90% loss of activity, protease II
65
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20 min, purified enzyme, inactivation
90
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pH 7.0, 30 min, complete inactivation, protease I
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Purified enzyme contains trace amounts of a serine proteinase which rapidly degrades the Staphylococcus aureus metalloproteinase when EDTA is present, no degradation occurs when Ca2+ is added
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange chromatography
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native enzyme by hydrophobic interaction and ion exchange chromatography
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protease I (pI: 4.0) and protease II (pI: 9.4)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aur, DNA and amino acid sequence determination and analysis, expression analysis and genetic survey of the prevalence of extracellular protease-encoding genes in genomes of 167 commensal and pathogenic strains of Staphylococcus aureus, overview. Gene expression and secretion of the enzyme in the course of human and mouse infection, PDR-based expression analysis
gene aur, encoding the enzyme, is regulated by the genes sarA, rot, and agr, the latter encoding RNAIII, agr and mgr A stimulate enzyme expression, while rot and sar A suppress it, mutational analysis and expression analysis, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T85R/L86Y
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mutation at the site of autocatalytic activation in the propeptide. Mutation results in secretion of an intact N-terminal propeptide with degradation of the M4 metalloprotease domain. The segment of the fungalysin-thermolysin-propeptide domain promotes intracellular processing of proaureolysin while bestowing a chaperone function
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine