Abstract:
:The intrinsic fluorescence of potato tuber pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) was used as an indicator of conformational changes due to ligand binding. Binding of the substrates and the allosteric activator fructose-2,6-bisphosphate was quantitatively compared to their respective kinetic effects on enzymatic activity. PFP exhibited a relatively high affinity for its isolated substrates, relative to the enzyme's respective K(m) (substrate) values. There are two distinct types of fructose-1,6-bisphosphate interaction with PFP, corresponding to catalytic and activatory binding. Activatory fructose-1,6-bisphosphate binding shares several characteristics with fructose-2,6-bisphosphate binding, indicating that both ligands compete for the same allosteric activator site. Activation by fructose-1,6-bisphosphate or fructose-2,6-bisphosphate was exerted primarily on the forward (glycolytic) reaction by greatly increasing the enzyme's affinity for fructose-6-phosphate. Binding of substrates and effectors to PFP and PFP kinetic properties were markedly influenced by assay pH. Results indicate an increased glycolytic role for PFP during cytosolic acidification that accompanies anoxia stress.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Podestá FE,Plaxton WCdoi
10.1016/s0003-9861(03)00157-7subject
Has Abstractpub_date
2003-06-01 00:00:00pages
101-7issue
1eissn
0003-9861issn
1096-0384pii
S0003986103001577journal_volume
414pub_type
杂志文章abstract::The effect of hydroperoxides on hematin-catalyzed initiation and propagation of lipid peroxidation was examined utilizing soybean phosphatidylcholine liposomes as model membranes. Polarographic and spectrophotometric methods revealed a bimodal pseudocatalytic activity for hematin. A slow initiation phase of peroxidati...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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abstract::Peroxynitrite is a strong oxidant that reacts with a variety of biomolecules in vivo and in vitro. When rat thymocytes in phosphate buffer are exposed to 25 microM peroxynitrite for 10 min, DNA single strand breaks (SSB) can be detected. These SSB are repaired if the cells are incubated in fresh media at 37 degrees C ...
journal_title:Archives of biochemistry and biophysics
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doi:10.1006/abbi.1996.0418
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