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 (Comment) | Organism |
---|---|
- |
Escherichia coli |
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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.006 | - |
prolipoprotein | diacylglyceryl-modified murein prolipoprotein | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasmic membrane | integral protein | Escherichia coli | - |
- |
cytoplasmic membrane | membrane topology of the enzyme | Escherichia coli | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no requirement for divalent cation | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
18140 | - |
E. coli, calculation from nucleotide sequence | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
B | - |
Escherichia coli B / ATCC 11303 | - |
B | - |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Escherichia coli |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
37°C: activity maximum, active even at 80°C | Escherichia coli |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Escherichia coli |