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Literature summary extracted from

  • Sankaran, K.
    Signal peptidase II (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 201-204.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.23.36 detergent required for activity, e.g. Triton X-100 or Nikkol, but not lauryl sarcoside or octylglucoside Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.36 DNA and amino acid sequence determination and analysis Staphylococcus aureus
3.4.23.36 DNA and amino acid sequence determination and analysis Pseudomonas fluorescens
3.4.23.36 DNA and amino acid sequence determination and analysis Klebsiella aerogenes
3.4.23.36 enzyme overexpression in Escherichia coli confers high resistance to globomycin Myxococcus xanthus
3.4.23.36 gene lsp, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli under control of the trp promoter Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.36 Globomycin
-
Bacillus subtilis
3.4.23.36 Globomycin uncompetitive Escherichia coli
3.4.23.36 Globomycin
-
Klebsiella aerogenes
3.4.23.36 Globomycin
-
Myxococcus xanthus
3.4.23.36 Globomycin
-
Pseudomonas fluorescens
3.4.23.36 Globomycin
-
Staphylococcus aureus
3.4.23.36 HgCl2
-
Escherichia coli
3.4.23.36 lauroyl sarcoside
-
Escherichia coli
3.4.23.36 octylglucoside
-
Escherichia coli
3.4.23.36 tosyl arginyl methyl ester
-
Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.36 inner membrane
-
Staphylococcus aureus
-
-
3.4.23.36 inner membrane
-
Bacillus subtilis
-
-
3.4.23.36 inner membrane
-
Pseudomonas fluorescens
-
-
3.4.23.36 inner membrane
-
Klebsiella aerogenes
-
-
3.4.23.36 inner membrane
-
Myxococcus xanthus
-
-
3.4.23.36 inner membrane transmembrane protein with a large and a small loop at the periplasmic side Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Staphylococcus aureus
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Bacillus subtilis
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Escherichia coli
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Pseudomonas fluorescens
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Klebsiella aerogenes
3.4.23.36 additional information no requirement for metal ions, thiol reagents, and phospholipids Myxococcus xanthus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.36 18000
-
x * 18144, amino acid sequence calculation, x * 18000, SDS-PAGE Escherichia coli
3.4.23.36 18144
-
x * 18144, amino acid sequence calculation, x * 18000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.36 bacterial lipoprotein + H2O Staphylococcus aureus cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O Bacillus subtilis cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O Escherichia coli cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O Pseudomonas fluorescens cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O Klebsiella aerogenes cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O Myxococcus xanthus cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.36 Bacillus subtilis
-
-
-
3.4.23.36 Escherichia coli
-
gene lsp
-
3.4.23.36 Klebsiella aerogenes
-
-
-
3.4.23.36 Myxococcus xanthus
-
-
-
3.4.23.36 Pseudomonas fluorescens
-
-
-
3.4.23.36 Staphylococcus aureus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.36 additional information N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme Escherichia coli
3.4.23.36 proteolytic modification N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.36 native enzyme from inner membrane to homogeneity by solubilization from membrane with Triton X-100, heat treatmemt at 65°C and pH 4.0, anion exchange chromatography, and chromatofocusing, 35000fold, recombinant enzyme by ammonium sulfate fractionation, anion exchange chromatography in presence of EDTA, and gel filtration to homogeneity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Staphylococcus aureus ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Bacillus subtilis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Escherichia coli ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Pseudomonas fluorescens ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Klebsiella aerogenes ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Myxococcus xanthus ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Staphylococcus aureus ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Bacillus subtilis ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Escherichia coli ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Pseudomonas fluorescens ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Klebsiella aerogenes ?
-
?
3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Myxococcus xanthus ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Staphylococcus aureus ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Bacillus subtilis ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Escherichia coli ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Pseudomonas fluorescens ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Klebsiella aerogenes ?
-
?
3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Myxococcus xanthus ?
-
?
3.4.23.36 additional information active site catalytic residues are Asp102 and Asp129 Bacillus subtilis ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.23.36 ? x * 18144, amino acid sequence calculation, x * 18000, SDS-PAGE Escherichia coli
3.4.23.36 More primary structure Staphylococcus aureus
3.4.23.36 More primary structure Escherichia coli
3.4.23.36 More primary structure Pseudomonas fluorescens
3.4.23.36 More primary structure Klebsiella aerogenes

Synonyms

EC Number Synonyms Comment Organism
3.4.23.36 lipoprotein-specific signal peptidase
-
Escherichia coli
3.4.23.36 More the enzyme belongs to the A8 peptidase family Staphylococcus aureus
3.4.23.36 More the enzyme belongs to the A8 peptidase family Bacillus subtilis
3.4.23.36 More the enzyme belongs to the A8 peptidase family Escherichia coli
3.4.23.36 More the enzyme belongs to the A8 peptidase family Pseudomonas fluorescens
3.4.23.36 More the enzyme belongs to the A8 peptidase family Klebsiella aerogenes
3.4.23.36 More the enzyme belongs to the A8 peptidase family Myxococcus xanthus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.23.36 80
-
purified enzyme, stable for a short time Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.36 additional information
-
neutral pH optimum Staphylococcus aureus
3.4.23.36 additional information
-
neutral pH optimum Bacillus subtilis
3.4.23.36 additional information
-
neutral pH optimum Pseudomonas fluorescens
3.4.23.36 additional information
-
neutral pH optimum Klebsiella aerogenes
3.4.23.36 additional information
-
neutral pH optimum Myxococcus xanthus
3.4.23.36 6
-
purified enzyme Escherichia coli
3.4.23.36 7.9
-
crude enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.23.36 additional information no requirement for cofactors Staphylococcus aureus
3.4.23.36 additional information no requirement for cofactors Bacillus subtilis
3.4.23.36 additional information no requirement for cofactors Escherichia coli
3.4.23.36 additional information no requirement for cofactors Pseudomonas fluorescens
3.4.23.36 additional information no requirement for cofactors Klebsiella aerogenes
3.4.23.36 additional information no requirement for cofactors Myxococcus xanthus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.23.36 0.000036
-
Globomycin
-
Escherichia coli