BRENDA - Enzyme Database show
show all sequences of 3.4.23.36

Bacterial prolipoprotein signal peptidase

Sankaran, K.; Wu, H.C.; Methods Enzymol. 248, 169-180 (1995)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
detergent
detergent required for optimal activity in vitro, Triton X-100 and Nikkol support activity
Escherichia coli
additional information
no requirement for phospholipid
Escherichia coli
Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
General Stability
General Stability
Organism
Unstable during purification unless 10% glycerol, 1% Triton X-100, and 1 mM DTT are included in the buffers
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
chymostatin
-
Escherichia coli
Globomycin
noncompetitive
Escherichia coli
HgCl2
-
Escherichia coli
NEM
-
Escherichia coli
octylglucoside
1%, complete inactivation
Escherichia coli
pepstatin
-
Escherichia coli
Phenylethyl alcohol
-
Escherichia coli
phenylmethylsulfonyl fluoride
-
Escherichia coli
tosyl-Arg methyl ester
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
prolipoprotein
diacylglyceryl-modified murein prolipoprotein
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasmic membrane
integral protein; membrane topology of the enzyme
Escherichia coli
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no requirement for divalent cation
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18140
-
E. coli, calculation from nucleotide sequence
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
processing of the lipid-modified prolipoproteins
?
-
-
-
additional information
Escherichia coli B / ATCC 11303
processing of the lipid-modified prolipoproteins
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
B
-
Escherichia coli B / ATCC 11303
-
B
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Storage Stability
Storage Stability
Organism
4C or -20C, 10% glycerol, 1% Triton X-100, and 1 mM DTT, stable for at least 1 month
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein
30813
Escherichia coli
?
-
-
-
-
additional information
processing of the lipid-modified prolipoproteins
30813
Escherichia coli
?
-
-
-
-
additional information
indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
additional information
processing of the lipid-modified prolipoproteins
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
Murein prolipoprotein + H2O
cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites
30813
Escherichia coli
?
-
-
-
-
Murein prolipoprotein + H2O
cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Escherichia coli
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
additional information
-
37C: activity maximum, active even at 80C
Escherichia coli
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
in presence of 2% Triton X-100 enzyme can withstand brief exposure up to
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
detergent
detergent required for optimal activity in vitro, Triton X-100 and Nikkol support activity
Escherichia coli
additional information
no requirement for phospholipid
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
General Stability (protein specific)
General Stability
Organism
Unstable during purification unless 10% glycerol, 1% Triton X-100, and 1 mM DTT are included in the buffers
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
chymostatin
-
Escherichia coli
Globomycin
noncompetitive
Escherichia coli
HgCl2
-
Escherichia coli
NEM
-
Escherichia coli
octylglucoside
1%, complete inactivation
Escherichia coli
pepstatin
-
Escherichia coli
Phenylethyl alcohol
-
Escherichia coli
phenylmethylsulfonyl fluoride
-
Escherichia coli
tosyl-Arg methyl ester
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
prolipoprotein
diacylglyceryl-modified murein prolipoprotein
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasmic membrane
integral protein; membrane topology of the enzyme
Escherichia coli
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no requirement for divalent cation
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18140
-
E. coli, calculation from nucleotide sequence
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
processing of the lipid-modified prolipoproteins
?
-
-
-
additional information
Escherichia coli B / ATCC 11303
processing of the lipid-modified prolipoproteins
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Storage Stability (protein specific)
Storage Stability
Organism
4C or -20C, 10% glycerol, 1% Triton X-100, and 1 mM DTT, stable for at least 1 month
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein
30813
Escherichia coli
?
-
-
-
-
additional information
processing of the lipid-modified prolipoproteins
30813
Escherichia coli
?
-
-
-
-
additional information
indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
additional information
processing of the lipid-modified prolipoproteins
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
Murein prolipoprotein + H2O
cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites
30813
Escherichia coli
?
-
-
-
-
Murein prolipoprotein + H2O
cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites
30813
Escherichia coli B / ATCC 11303
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Escherichia coli
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
additional information
-
37C: activity maximum, active even at 80C
Escherichia coli
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
in presence of 2% Triton X-100 enzyme can withstand brief exposure up to
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Escherichia coli
Other publictions for EC 3.4.23.36
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
717100
Xiao
Myxobacteria antibiotic TA (my ...
Escherichia coli
Antimicrob. Agents Chemother.
56
2014-2021
2012
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
708786
Schmaler
Staphylococcal lipoproteins an ...
Staphylococcus aureus
Int. J. Med. Microbiol.
300
155-160
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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1
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
708937
Vickerman
A genetic determinant in Strep ...
Streptococcus gordonii
J. Bacteriol.
192
2535-2545
2010
-
-
1
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
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-
-
-
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1
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1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
707166
Banaei
Lipoprotein processing is esse ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Antimicrob. Agents Chemother.
53
3799-3802
2009
-
-
-
-
-
-
-
-
-
-
-
2
-
163
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
708925
Das
Contribution of lipoproteins a ...
Streptococcus sanguinis, Streptococcus sanguinis SK36
J. Bacteriol.
191
4166-4179
2009
-
-
-
-
-
-
-
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
682007
Khandavilli
Maturation of Streptococcus pn ...
Streptococcus pneumoniae
Mol. Microbiol.
67
541-557
2008
-
-
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700533
Arimoto
Role of prolipoprotein diacylg ...
Streptococcus mutans
Oral Microbiol. Immunol.
23
515-519
2008
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680486
Rahman
The lspA gene, encoding the ty ...
Rickettsia typhi
J. Bacteriol.
189
336-341
2007
-
-
1
-
-
-
-
-
1
-
-
1
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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1
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-
-
-
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1
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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682822
Geukens
The type II signal peptidase o ...
Legionella pneumophila
Res. Microbiol.
157
836-841
2006
-
1
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668802
Sankaran
-
Signal peptidase II ...
Bacillus subtilis, Escherichia coli, Klebsiella aerogenes, Myxococcus xanthus, Pseudomonas fluorescens, Staphylococcus aureus
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
201-204
2004
1
-
5
-
-
-
10
-
6
6
2
6
-
6
-
2
1
-
-
-
-
-
19
5
-
-
1
-
7
-
-
6
1
-
-
1
-
5
6
-
-
-
-
10
1
-
6
6
2
6
-
-
2
1
-
-
-
-
19
5
-
-
1
-
7
-
-
-
-
-
-
-
-
-
670307
Sander
Lipoprotein processing is requ ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Mol. Microbiol.
52
1543-1552
2004
-
-
1
-
1
-
-
-
-
-
-
2
-
161
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
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-
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1
-
-
1
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-
-
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2
-
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-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670851
Gonnet
Fine-tuning the prediction of ...
Escherichia coli K-12
Proteomics
4
1597-1613
2004
-
-
-
-
-
-
-
-
-
-
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4
-
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1
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1
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-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
651951
Tjalsma
The potential active site of t ...
Bacillus subtilis
J. Biol. Chem.
274
28191-28197
1999
-
-
1
-
16
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30813
Sankaran
Bacterial prolipoprotein signa ...
Escherichia coli, Escherichia coli B / ATCC 11303
Methods Enzymol.
248
169-180
1995
2
-
1
-
-
1
9
1
1
1
1
2
-
177
-
-
1
-
-
-
-
1
6
-
1
1
1
-
1
-
-
-
-
-
-
2
-
1
-
-
-
1
-
9
-
1
1
1
1
2
-
-
-
1
-
-
-
1
6
-
1
1
1
-
1
-
-
-
-
-
-
-
-
-
30814
Zhao
Nucleotide sequence of the Sta ...
Staphylococcus aureus
FEBS Lett.
299
80-84
1992
-
-
1
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
-
-
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30809
Isaki
Cloning and nucleotide sequenc ...
Klebsiella aerogenes
J. Bacteriol.
172
469-472
1990
-
-
1
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
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Dev
Signal peptidases and signal p ...
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1990
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30808
Innis
Nucleotide sequence of the Esc ...
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Proc. Natl. Acad. Sci. USA
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1984
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30810
Yu
Nucleotide sequence of the lsp ...
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1984
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30811
Yamada
The major outer membrane lipop ...
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FEBS Lett.
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1984
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