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Literature summary for 3.4.23.36 extracted from
- Bacterial prolipoprotein signal peptidase (1995), Methods Enzymol., 248, 169-180.
Activating Compound
| Activating Compound | Comment | 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)
| Cloned (Comment) | 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 | Comment | 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 | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.006 | - |
prolipoprotein | diacylglyceryl-modified murein prolipoprotein | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasmic membrane | integral protein | Escherichia coli | - |
- |
| cytoplasmic membrane | membrane topology of the enzyme | Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no requirement for divalent cation | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 18140 | - |
E. coli, calculation from nucleotide sequence | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
B | - |
| Escherichia coli B / ATCC 11303 | - |
B | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C or -20°C, 10% glycerol, 1% Triton X-100, and 1 mM DTT, stable for at least 1 month | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Escherichia coli | ? | - |
? | |
| additional information | processing of the lipid-modified prolipoproteins | 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 | Escherichia coli B / ATCC 11303 | ? | - |
? | |
| additional information | processing of the lipid-modified prolipoproteins | 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 | 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 | Escherichia coli B / ATCC 11303 | ? | - |
? | |
| prolipoprotein + H2O | - |
Escherichia coli | ? | - |
? | |
| prolipoprotein + H2O | - |
Escherichia coli B / ATCC 11303 | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Escherichia coli |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
37°C: activity maximum, active even at 80°C | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | 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 | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Escherichia coli |
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