Application | Comment | Organism |
---|---|---|
pharmacology | the enzyme ia a target for development of drugs in therapy of Lyme disease caused by Borrelia burgdorferi | Borreliella burgdorferi |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,10-phenanthroline | complete inhibition at 0.25 mM, reversible by Zn2+, not by other divalent cations, overview | Borreliella burgdorferi | |
bestatin | complete inhibition at 0.1 mM, not reversible by divalent cations | Borreliella burgdorferi | |
EDTA | 50% inhibition at 10 mM, reversible by divalent cations, best by Zn2+ | Borreliella burgdorferi | |
additional information | no or poor inhibition by PMSF, E64, TLCK, pepstatin A, and leupeptin | Borreliella burgdorferi |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | dependent on | Borreliella burgdorferi |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
6 * 50000, SDS-PAGE | Borreliella burgdorferi |
300000 | - |
gel filtration | Borreliella burgdorferi |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Borreliella burgdorferi | the enzyme is probably involved in amino acid supply in the organism deficient in amino acid synthesis pathways, and/or in peptide and/or protein processing | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Borreliella burgdorferi | O51096 | gene BB0069 | - |
Purification (Comment) | Organism |
---|---|
native enzyme 32fold to homogeneity by anion exchange chromatography and gel filtration | Borreliella burgdorferi |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.001 | - |
purified enzyme | Borreliella burgdorferi |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Leu-7-amido-4-methylcoumarin + H2O | - |
Borreliella burgdorferi | L-Leu + 7-amino-4-methylcoumarin | - |
? | |
additional information | the enzyme is probably involved in amino acid supply in the organism deficient in amino acid synthesis pathways, and/or in peptide and/or protein processing | Borreliella burgdorferi | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | 6 * 50000, SDS-PAGE | Borreliella burgdorferi |
More | oligomerization is required for activity, the monomer is inactive, the enzyme contains no disulfide bonds, peptide mass fingerprinting, overview | Borreliella burgdorferi |
Synonyms | Comment | Organism |
---|---|---|
aminopeptidase II | - |
Borreliella burgdorferi |
More | the enzyme is a member of the M29 family of metallopeptidases | Borreliella burgdorferi |
TAP | - |
Borreliella burgdorferi |
thermophilic aminopeptidase | - |
Borreliella burgdorferi |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
- |
Borreliella burgdorferi |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermal inactivation through transition of the hexameric to the monomeric form | Borreliella burgdorferi |
25 | 50 | purified enzyme, completely stable for 240 min | Borreliella burgdorferi |
60 | - |
purified enzyme, no loss activity within 10 min, 240 min: loss of 12.5% activity | Borreliella burgdorferi |
70 | - |
purified enzyme, loss of 75% activity within 10 min, 240 min: loss of 91% activity | Borreliella burgdorferi |
100 | - |
purified enzyme, 10 min, complete inactivation | Borreliella burgdorferi |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Borreliella burgdorferi |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | 20% of maximal activity at pH 6.0, 50% at pH 9.0 | Borreliella burgdorferi |