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Literature summary for 3.4.11.10 extracted from

  • Bertin, P.B.; Lozzi, S.P.; Howell, J.K.; Restrepo-Cadavid, G.; Neves, D.; Teixeira, A.R.L.; De Sousa, M.V.; Norris, S.J.; Santana, J.M.
    The thermophilic, homohexameric aminopeptidase of Borrelia burgdorferi is a member of the M29 family of metallopeptidases (2005), Infect. Immun., 73, 2253-2261.
    View publication on PubMedView publication on EuropePMC

Application

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

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

Metals/Ions Comment Organism Structure
Zn2+ dependent on Borreliella burgdorferi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
6 * 50000, SDS-PAGE Borreliella burgdorferi
300000
-
gel filtration Borreliella burgdorferi

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Borreliella burgdorferi O51096 gene BB0069
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 32fold to homogeneity by anion exchange chromatography and gel filtration Borreliella burgdorferi

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.001
-
purified enzyme Borreliella burgdorferi

Substrates and Products (Substrate)

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

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Borreliella burgdorferi

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Borreliella burgdorferi

pH Range

pH Minimum pH Maximum Comment Organism
6 9 20% of maximal activity at pH 6.0, 50% at pH 9.0 Borreliella burgdorferi