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d-Amino acid oxidase and presence of d-proline in Xenopus laevis
Comparative Biochemistry and Physiology Part 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
Hiroki, Soma +6 more
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A radioisotopic assay for proline oxidase activity.
The Journal of laboratory and clinical medicine, 1975We developed a radioisotopic assay for proline oxidase in which product deltal-pyrroline-5-carboxylate-14-C is reacted with o-aminobenzaldehyde and the radioactivity trapped as the dihydroquinazolinium compound is recovered by ion-exchange chromatography.
J M, Phang +3 more
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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 ...
Tallarita E. +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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Hydroxy-L-proline as a substrate for HOG kidney D-amino acid oxidase
Biochemical and Biophysical Research Communications, 1974Summary In contrast to earlier findings, hydroxy-L-proline is oxidized by hog kidney D-amino acid oxidase, with a V max comparable to that of L-proline but with a somewhat higher K. Kinetic constants and pH-dependency data are in reported both for hydroxy-L-proline and allohydroxy-D-proline.
A M, Heacock, E, Adams
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Cancer research, 2001
The p53-dependent initiation of apoptosis is accompanied by the induction of proline oxidase (POX), a mitochondrial enzyme catalyzing the conversion of proline to pyrroline-5-carboxylate with the concomitant transfer of electrons to cytochrome c. However, the contribution of increased POX activity to apoptosis, if any, remains unknown. Using Adriamycin
S P, Donald +6 more
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The p53-dependent initiation of apoptosis is accompanied by the induction of proline oxidase (POX), a mitochondrial enzyme catalyzing the conversion of proline to pyrroline-5-carboxylate with the concomitant transfer of electrons to cytochrome c. However, the contribution of increased POX activity to apoptosis, if any, remains unknown. Using Adriamycin
S P, Donald +6 more
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[The proline oxidase complex].
Biochemische Zeitschrift, 2000K, LANG, H, LANG
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Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation
Nature Reviews Molecular Cell Biology, 2010David U Mick +2 more
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