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evolution
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
evolution
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XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
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evolution
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XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
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evolution
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XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
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evolution
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XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
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evolution
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XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
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malfunction
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decreased serum prolidase activity and increased oxidative stress are correlated in early pregnancy loss, overview
malfunction
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enzyme activity is increased in aortic dilatation compared to controls
malfunction
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enzyme activity is increased in patients with nonalcoholic steatohepatitis, NASH, compared to controls, significant correlation between serum prolidase enzyme activity and fibrosis score in patients with NASH
malfunction
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increased PSR activity in case of colitis
malfunction
misfunctioning causes prolidase deficiency, a recessive connective tissue disorder characterized by severe skin lesions, mental retardation and respiratory tract infections
malfunction
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prolidase activity is significantly increased in patients with thalassemia major compared to the controls, relationship between prolidase activity and oxidative status in patients with thalassemia major, overview
malfunction
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prolidase deficiency is a rare autosomal recessive disorder that affects the connective tissue. Symptoms of prolidase deficiency include skin lesions, mental retardation and recurrent respiratory infections. Prolidase is linked to collagen metabolism and is associated with melanoma. Prolidase is essential for collagen breakdown and the lack of this enzyme results in serious skin abnormalities. While an increase in prolidase activity and a decrease in collagen in breast cancer tissue may cause increased cancer risk. Recombinant human prolidase is used for enzyme replacement therapy
malfunction
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prolidase deficiency is a rare, pan-ethnic, autosomal recessive disease with a broad phenotypic spectrum
malfunction
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prolidase may play a role in angiogenesis
malfunction
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serum prolidase activity and oxidative stress are significantly associated with the presence of etal growth restriction, the correlation between serum prolidase activity and markers of oxidative stress are represented as increased serum total oxidative status level and decreased serum total antioxidant capacity and total free sulfhydryl levels, suggesting an association of collagen turnover and oxidative stress in vascular dysfunction, overview
metabolism
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prolidase catalyzes the final step of collagen degradation
metabolism
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prolidase catalyzes the final step of collgane breakdown, releasing free proline for collagen recycling
metabolism
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prolidase plays an important role in collagen metabolism, matrix remodeling and cell growth. Additionally, the final step of collagen degradation in the extracellular matrix is mediated by prolidase
metabolism
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the enzyme is important in the collagen metabolism, overview
physiological function
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OPAA-2 is active in detoxification of organophosphorus compounds, the nerve agents GB, sarin or O-isopropyl methylphosphonofluoridate, VX and blister agent HD, a sulfur mustard, overview
physiological function
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prolidase activity may be a step-limiting factor in the regulation of collagen biosynthesis
physiological function
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prolidase is a marker of collagen turnover. The enzyme activity is higher in women with early pregnancy loss than in those without. Collagen turnover is increased in patients with early pregnancy loss and may be an etiopathological factor of this disease
physiological function
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prolidase is a specific imidodipeptidase involved in collagen degradation
physiological function
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prolidase plays an important role in collagen metabolism, matrix remodeling and cell growth. Additionally, the final step of collagen degradation in the extracellular matrix is mediated by prolidase
physiological function
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
physiological function
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isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
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physiological function
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isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
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physiological function
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isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
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physiological function
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isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
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physiological function
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isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
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physiological function
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OPAA-2 is active in detoxification of organophosphorus compounds, the nerve agents GB, sarin or O-isopropyl methylphosphonofluoridate, VX and blister agent HD, a sulfur mustard, overview
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