Identifying the structure of the active sites of human recombinant prolidase |
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Authors: | Roberta Besio Stefania Alleva Antonella Forlino Anna Lupi Carlo Meneghini Velia Minicozzi Antonella Profumo Francesco Stellato Ruggero Tenni Silvia Morante |
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Institution: | 1. Dipartimento di Biochimica Sez. Medicina e Farmacia, Università di Pavia, Pavia, Italy 2. Dipartimento di Fisica and INFN, Università di Roma “Tor Vergata”, Rome, Italy 3. Dipartimento di Fisica, Università di Roma Tre, Rome, Italy 4. Dipartimento di Chimica, Università di Pavia, Pavia, Italy
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Abstract: | In this paper we provide a detailed biochemical and structural characterization of the active site of recombinant human prolidase,
a dimeric metalloenzyme, whose misfunctioning causes a recessive connective tissue disorder (prolidase deficiency) characterized
by severe skin lesions, mental retardation and respiratory tract infections. It is known that the protein can host two metal
ions in the active site of each constituent monomer. We prove that 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. Structural information
extracted from X-ray absorption spectroscopy measurements have been used to yield a full reconstruction of the atomic environment
around each one of the two monomeric active sites. In particular, as for the metal ion occupation configuration of the recombinant
human prolidase, we have found that 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. |
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