PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2713125-4 1989 Following this novel step, prolidase retains full activity, obviating the requirement for preincubation of each enzyme fraction with Mn2+ prior to assay. Manganese(2+) 133-137 peptidase D Homo sapiens 27-36 2924773-4 1989 Analysis of inhibitor action and consideration of X-ray crystallographic data of relevant Mn2+ complexes allowed the active-site model of prolidase to be further refined; a new model is presented in which the substrate acts as a bidentate ligand towards the active-site manganous ion. Manganese(2+) 90-94 peptidase D Homo sapiens 138-147 6429439-4 1984 Control prolidase was stable to prolonged preincubation with Mn2+, whereas the abnormal prolidase was progressively inactivated. Manganese(2+) 61-65 peptidase D Homo sapiens 8-17 3139929-3 1988 Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+. Manganese(2+) 315-319 peptidase D Homo sapiens 39-48 6692525-1 1984 We describe here an easy method of determining prolidase (EC 3.4.13.9) in plasma after preincubation with Mn2+ for 24 h at 37 degrees C to maximize prolidase activity. Manganese(2+) 106-110 peptidase D Homo sapiens 47-56 3139929-1 1988 Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+. Manganese(2+) 116-120 peptidase D Homo sapiens 0-9 3139929-1 1988 Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+. Manganese(2+) 181-185 peptidase D Homo sapiens 0-9 3139929-1 1988 Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+. Manganese(2+) 181-185 peptidase D Homo sapiens 0-9 3139929-3 1988 Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+. Manganese(2+) 174-178 peptidase D Homo sapiens 242-251 21425789-4 2011 With the purpose of identifying which is the most efficient dimetallic center for the prolidase catalyzed reaction, Zn(II), Co(II), and Mn(II) have been examined as potential catalytic metals for this enzyme. Manganese(2+) 136-142 peptidase D Homo sapiens 86-95 7139961-4 1982 In addition, the reaction mixture was preincubated with Mn2+ for 24 h in order to triple prolidase activity. Manganese(2+) 56-60 peptidase D Homo sapiens 89-98 21699887-7 2011 RESULTS: An activation step consisting in prolidase incubation with 1 mmol/l MnCl(2) and 0.75 mmol/l reduced glutathione at 50 C for 20 min was necessary to obtain the maximum activity and to accurately determine, for the recombinant enzyme, V(max) (489 U/mg), K(m) (5.4 mM) and Mn(2+) affinity (54 mM(-1)). Manganese(2+) 279-285 peptidase D Homo sapiens 42-51 22999980-0 2013 A Mn(II)-Mn(II) center in human prolidase. Manganese(2+) 2-8 peptidase D Homo sapiens 32-41 22999980-0 2013 A Mn(II)-Mn(II) center in human prolidase. Manganese(2+) 9-15 peptidase D Homo sapiens 32-41 22999980-3 2013 Here, using EPR and ICP-MS on human recombinant prolidase produced in Escherichia coli (hRecProl), the Mn(II) ion organized in a dinuclear Mn(II)-Mn(II) center was identified as the protein cofactor. Manganese(2+) 103-109 peptidase D Homo sapiens 48-57 7817771-2 1994 These peaks of prolidase isozymes I and II differed from each other in their responses to preincubation with Mn2+, their substrate specificity, optimal pH, and heat stability. Manganese(2+) 109-113 peptidase D Homo sapiens 15-24