Organic and inorganic substrates as probes for comparing native bovine lactoperoxidase and recombinant human myeloperoxidase.
The interaction of native bovine lactoperoxidase (nbLPO) with four substrates has been studied and compared with that of recombinant human myeloperoxidase (rhMPO). Kinetic, spectroscopic and binding parameters extrapolated for each enzyme-substrate adduct have been interpreted in the light of the structural data available for myeloperoxidase (X-ray structure) and lactoperoxidase (3D-model), respectively. The differences in the reactivity and affinity of nbLPO and rhMPO towards SCN(-), catechol, dopamine and 3,4-dihydroxyphenylpropionic acid are here discussed and related to a different structure of the organic substrate access channel as well as to a different accessibility of the heme pocket in the two enzymes.
Ghibaudi
Elena
E
Dipartimento di Chimica IFM, Università di Torino, Via P. Giuria 7, I-10125, Torino, Italy. elena.ghibaudi@unito.it
Laurenti
Enzo
E
Pacchiardo
Cristina
C
Suriano
Gianpaolo
G
Moguilevsky
Nicole
N
Pia Ferrari
Rosa
R
D000818:Animals; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007784:Lactoperoxidase / Q000737:chemistry / Q000378:metabolism*; D015335:Molecular Probes; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D015335:Molecular Probes; D011994:Recombinant Proteins; D007784:Lactoperoxidase; D009195:Peroxidase