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Literature summary for 3.4.11.1 extracted from

  • Cappiello, M.; Alterio, V.; Amodeo, P.; Del Corso, A.; Scaloni, A.; Pedone, C.; Moschini, R.; De Donatis, G.M.; De Simone, G.; Mura, U.
    Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase (2006), Biochemistry, 45, 3226-3234.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
Zn2+-Zn2+-enzyme in complex with the peptidomimetic derivative zofenoprilat, soaking of crystals in 20 mM zofenoprilat, X-ray diffraction structure determination and analysis at 1.85 A resolution Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
Cys-Gly inhibits the activity of the Zn2+-Zn2+-enzyme with substrate Leu-Gly competitively Bos taurus
Leu-Gly inhibits the activity of the Mn2+-Zn2+-enzyme with substrate Cys-Gly competitively Bos taurus
zofenoprilat competitive versus Leu-Gly with the Zn2+-Zn2+-enzyme, uncompetitive with the Mn2+-Zn2+-enzyme, binding structure analysis Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview Bos taurus
Mg2+ two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview Bos taurus
Mn2+ Km is 0.00056 mM with substrate Cys-Gly, two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview Bos taurus
additional information metallopeptidase Bos taurus
Zn2+ two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00727
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of Zn2+-Zn2+-enzyme and Mn2+-Zn2+-enzyme, by ethanol precipitation, and gel filtration to homogeneity Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Bos taurus
-

Storage Stability

Storage Stability Organism
-80°C, purified enzyme, in 10 mM sodium phosphate, pH 7.8, 0.02 M magnesium acetate, 2 mM DTT, and 0.05 mM manganese chloride, stable for at least 2 months Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cys-Gly + H2O only hydrolyzed by the Mn2+-Zn2+-enzyme, not by the Zn2+-Zn2+-enzyme Bos taurus Cys + Gly
-
?
Leu-Gly + H2O substrate of the Mn2+-Zn2+-enzyme and the Zn2+-Zn2+-enzyme Bos taurus Leu + Gly
-
?
additional information the enzyme prefers peptide substrates with bulky and hydrophobic N-terminal amino acid residues Bos taurus ?
-
?

Synonyms

Synonyms Comment Organism
LAP
-
Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0008
-
zofenoprilat Zn2+-Zn2+-enzyme, versus substrate Leu-Gly Bos taurus
0.0164
-
Cys-Gly Mn2+-Zn2+-enzyme, versus substrate Leu-Gly Bos taurus
0.65
-
Leu-Gly Z2+-Zn2+-enzyme, versus substrate Cys-Gly Bos taurus
1.1
-
zofenoprilat Mn2+-Zn2+-enzyme, with substrate Leu-Gly Bos taurus
1.3
-
zofenoprilat Mn2+-Zn2+-enzyme, with substrate Cys-Gly Bos taurus