PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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	
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	
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