PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14580160-4 2003 The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2. glycylproline 249-262 peptidase D Homo sapiens 16-25 14580160-5 2003 The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2. glycylproline 36-49 peptidase D Homo sapiens 16-25 14580160-6 2003 The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2. glycylproline 141-154 peptidase D Homo sapiens 16-25 11680815-3 2001 The susceptibility of MEL-PRO to the action of prolidase was found to be similar, compared to glycyl-proline--the most abundant, endogenous substrate for prolidase and about 6-fold higher compared to its substrate--glycyl-hydroxyproline. glycylproline 94-108 peptidase D Homo sapiens 154-163 10582130-1 1999 Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins. glycylproline 0-16 peptidase D Homo sapiens 95-104 10582130-1 1999 Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins. glycylproline 18-25 peptidase D Homo sapiens 95-104 15378943-6 1994 RESULTS: Prolidase activity was found to be deficient, especially against gly-pro. glycylproline 74-81 peptidase D Homo sapiens 9-18 9972056-7 1998 It has been presented that product of synthesis, N-(anthraquinone-2-carbonyl)-L-proline evokes susceptibility to the action of purified prolidase, comparable to the susceptibility of glycyl-L-proline (standard substrate for prolidase). glycylproline 183-199 peptidase D Homo sapiens 136-145 1536787-2 1992 Prolidase activity of erythrocytes against substrate glycyl-proline was deficient, but after blood transfusions this was increased to 15.7% of donor activity and declined to 12% and 3.4% of normal activity after 8 and 45 days, respectively. glycylproline 53-67 peptidase D Homo sapiens 0-9 2317925-4 1990 The Km values for Gly-Pro of the control"s and the patient"s mother"s prolidase I were 2.90 +/- 0.22 and 2.88 +/- 0.27 mM, but the Vmax values for Gly-Pro of the mother"s enzyme was reduced about 30% compared to that of control enzymes (mother: 6.02 units/mg protein, control: 22.21 units/mg protein). glycylproline 18-25 peptidase D Homo sapiens 70-79 2073490-5 1990 The substrate specificity of partially purified prolidase-I and II in control fibroblasts was estimated against Gly-Pro, Ala-Pro, Met-Pro. glycylproline 112-119 peptidase D Homo sapiens 48-57 3205627-6 1988 As a consequence, the activity of prolidase in hemolysates increases to 159 mumol glycyl-L-proline hydrolyzed/h/ml compared to 5 mumol/h/ml for hemolysates of cells incubated in the absence of Mn++. glycylproline 82-98 peptidase D Homo sapiens 34-43 6743286-10 1984 At concentrations of the dipeptide that saturated prolidase, hydrolysis of glycyl-L-proline by whole cells was approximately 130 times slower than by lysates. glycylproline 75-91 peptidase D Homo sapiens 50-59 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+. glycylproline 66-73 peptidase D Homo sapiens 39-48 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+. glycylproline 66-73 peptidase D Homo sapiens 242-251 21425789-1 2011 The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis. glycylproline 32-39 peptidase D Homo sapiens 68-77 13174568-0 1954 Specificity of prolidase: effect of alterations in the pyrrolidine ring of glycyl-L-proline. glycylproline 75-91 peptidase D Homo sapiens 15-24 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). glycylproline 88-102 peptidase D Homo sapiens 77-86 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). glycylproline 104-106 peptidase D Homo sapiens 77-86 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. glycylproline 16-30 peptidase D Homo sapiens 54-63 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. glycylproline 16-30 peptidase D Homo sapiens 130-139 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. glycylproline 32-38 peptidase D Homo sapiens 54-63 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. glycylproline 32-38 peptidase D Homo sapiens 130-139 28942439-3 2017 We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase. glycylproline 163-177 peptidase D Homo sapiens 110-119 23549681-4 2013 However, in MDA-MB-231 cells (expressing high prolidase activity) cultured in the presence of prolidase substrates, Gly-Pro or Gly-HyPro, HIF-1alpha expression was induced in a dose-dependent manner, independently of estrogen receptor activation. glycylproline 116-123 peptidase D Homo sapiens 46-55 21425789-1 2011 The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis. glycylproline 32-39 peptidase D Homo sapiens 246-255 18550075-2 2008 The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated. glycylproline 214-221 peptidase D Homo sapiens 117-126 18550075-2 2008 The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated. glycylproline 214-221 peptidase D Homo sapiens 128-131 15804176-3 2005 RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95). glycylproline 63-81 peptidase D Homo sapiens 21-30 15804176-3 2005 RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95). glycylproline 63-81 peptidase D Homo sapiens 117-126 15804176-3 2005 RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95). glycylproline 83-90 peptidase D Homo sapiens 21-30 15804176-3 2005 RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95). glycylproline 83-90 peptidase D Homo sapiens 117-126 15530480-4 2004 RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine. glycylproline 36-49 peptidase D Homo sapiens 9-18 15530480-8 2004 CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2). glycylproline 39-52 peptidase D Homo sapiens 12-21 15530480-8 2004 CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2). glycylproline 39-52 peptidase D Homo sapiens 120-129 19263194-2 2009 The activity of prolidase I against glycylproline was strongly enhanced by D: -methionine. glycylproline 36-49 peptidase D Homo sapiens 16-25 16899234-8 2007 On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine. glycylproline 46-59 peptidase D Homo sapiens 19-28 16009141-4 2005 RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine. glycylproline 54-67 peptidase D Homo sapiens 27-36