Results 161 to 170 of about 29,796 (189)
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Proline oxidase inhibition by free fatty acids of rat pancreas
Biochimica Et Biophysica Acta - Biomembranes, 1980Proline oxidase activity was not measurable in pancreas homogenate but was measurable in pancreas slices. Moreover, added pancreas homogenate inhibited proline oxidase activity in rat liver mitochondria and several other tissues. The partially purified inhibitor from pancreas also inhibited the activity of glutamate, glucose 6-phosphate, NADH and ...
W Eugene Knox, W E Knox
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Expression in Escherichia coli of the catalytic domain of human proline oxidase
Protein Expression and Purification, 2012The human PRODH gene has been shown to have unique roles in regulating cell survival and apoptotic pathways and it has been related to velocardiofacial syndrome/DiGeorge syndrome and increased susceptibility to schizophrenia. It encodes for the flavoprotein proline oxidase (PO), which catalyzes the conversion of l-proline to Δ(1)-pyrroline-5 ...
Loredano Pollegioni +2 more
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d-Amino acid oxidase and presence of d-proline in Xenopus laevis
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 2013We purified D-amino acid oxidase (EC 1.4.3.3, DAO) from Xenopus laevis tadpoles. The optimal temperature and pH for enzyme activity were 35-40 °C and 8.3-9.0, respectively, depending on the substrate amino acids available to the enzyme; the highest activity was observed with D-proline followed by D-phenylalanine. Activity was significantly inhibited by
Yoko Nagata, Minoru Tanigawa
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Proline Oxidase (POX) as A Target for Cancer Therapy
Current Drug Targets, 2015Proline dehydrogenase/proline oxidase (PRODH/POX) is an enzyme catalyzing the first step of proline degradation, during which ROS and/or ATP is generated. POX is widely distributed in living organisms and is responsible for a number of regulatory processes such as redox homeostasis, osmotic adaptation, cell signaling and oxidative stress.
Konończuk, Joanna +5 more
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PROLINE OXIDASES IN HANSENULA SUBPELLICULOSA
Journal of Bacteriology, 1964Ling, Chung-Mei (Illinois Institute of Technology, Chicago), and L. R. Hedrick . Proline oxidases in Hansenula subpelliculosa . J. Bacteriol. 87: 1462–1470.
C M, LING, L R, HEDRICK
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Glucocorticoid control of hepatic proline oxidase
Metabolism, 1977Since adrenal corticosteroids are known to affect amino acid metabolism and gluconeogenesis, we examined the relationship of these hormones to hepatic proline oxidase, the mitochondrial enzyme degrading L-proline. In adrenalectomized rats hepatic proline oxidase activity decreased to about 50% of control levels within 5-6 days.
E M, Kowaloff, A S, Granger, J M, Phang
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Proline oxidase in cultured mammalian cells
Journal of Cellular Physiology, 1977AbstractWe sought a cultured cell line with Proline Oxidase activity to study the regulation and physiologic role of the enzyme in mammalian tissues. Among the cell lines tested, only LLC‐RK1 cells, derived from rabbit kidney, had significant Proline Oxidase activity; the Km for proline of the enzyme from these cells was similar to that for the liver ...
S J, Downing +4 more
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Characteristics of proline oxidase in rat tissues.
Journal of biochemistry, 1980In adult rats the activity of proline oxidase is high in the liver and kidney and moderate in the brain and heart, but it is not detectable in the lung, skeletal muscle, spleen, or small intestine. The activity in the liver is 1.5 times higher in females than males.
Y, Kawabata, N, Katunuma, Y, Sanada
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Glucocorticoid induction of proline oxidase in LLC‐RK1 cells
Journal of Cellular Physiology, 1978AbstractDexamethasone induced proline oxidase in cultured LLC‐RK1 cells, an epithelial cell line derived from rabbit kidney. The dexamethasone‐mediated increase in enzyme activity was concentration and time dependent. Although the effect could be dissociated from cell growth and cell density, it was dependent on protein and RNA synthesis.
E M, Kowaloff +3 more
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Epoxide derivatives of pipecolic acid and proline are inhibitors of pipecolate oxidase
Bioorganic & Medicinal Chemistry Letters, 1998The cis-4,5-epoxide derivative of L-pipecolic acid (2S,4S,5R-epoxypipecolic acid, cis-3) was synthesized and found to serve as an excellent substrate for L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented showing this compound is a mechanism-based inhibitor of L-PO, whereas 2S,3R,4S-
B, Ho, T M, Zabriskie
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