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Literature summary for 3.4.13.9 extracted from

  • Besio, R.; Alleva, S.; Forlino, A.; Lupi, A.; Meneghini, C.; Minicozzi, V.; Profumo, A.; Stellato, F.; Tenni, R.; Morante, S.
    Identifying the structure of the active sites of human recombinant prolidase (2010), Eur. Biophys. J., 39, 935-945.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-etrminally His-tagged enzyme in Escherichia coli strain BL21 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview Homo sapiens
additional information determination of enzyme samples metal contents, overview Homo sapiens
Zn2+ the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P12955
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
13.3
-
prolidase in presence of 10 mM Zn2+ Homo sapiens
158.3
-
prolidase in presence of 10 mM Mn2+ Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information human prolidase is the only metalloenzyme among the peptidases that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer structure comparison to the enzyme from Pyrococcus horikoshii OT3 prolidase, overview Homo sapiens

Synonyms

Synonyms Comment Organism
prolidase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction misfunctioning causes prolidase deficiency, a recessive connective tissue disorder characterized by severe skin lesions, mental retardation and respiratory tract infections Homo sapiens