The Experts below are selected from a list of 51 Experts worldwide ranked by ideXlab platform
In Kook Park - One of the best experts on this subject based on the ideXlab platform.
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Pyridoxal Phosphate inhibits the group I intron splicing
Molecular and Cellular Biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene ( td ). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg^2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg^2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K _i of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K _m and decreases in V _max values. (Mol Cell Biochem xxx: 17–34, 2005)
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Pyridoxal Phosphate inhibits the group I intron splicing.
Molecular and cellular biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene (td). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K(i) of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K(m) and decreases in V(max) values.
Chul Jung - One of the best experts on this subject based on the ideXlab platform.
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Pyridoxal Phosphate inhibits the group I intron splicing
Molecular and Cellular Biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene ( td ). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg^2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg^2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K _i of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K _m and decreases in V _max values. (Mol Cell Biochem xxx: 17–34, 2005)
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Pyridoxal Phosphate inhibits the group I intron splicing.
Molecular and cellular biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene (td). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K(i) of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K(m) and decreases in V(max) values.
Edith Wilson Miles - One of the best experts on this subject based on the ideXlab platform.
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Subunit Assembly in the Tryptophan Synthase α2β2 Complex STABILIZATION BY Pyridoxal Phosphate ALDIMINE INTERMEDIATES
The Journal of biological chemistry, 1995Co-Authors: Utpal Banik, S. Ashraf Ahmed, Peter Mcphie, Edith Wilson MilesAbstract:Abstract This work is aimed at understanding subunit assembly in the tryptophan synthase α2β2 complex and the importance of the internal aldimine between Pyridoxal Phosphate and lysine 87 of the β2 subunit of tryptophan synthase for subunit association. We utilize a mutant form of the β2 subunit that is unable to form the internal aldimine because lysine 87 is replaced by threonine (K87T). The K87T α2β2 complex is inactive in reactions catalyzed by the β2 subunit but retains activity in the reaction catalyzed by the α subunit. We find that dialysis removes Pyridoxal Phosphate much more rapidly from the K87T β2 subunit and α2β2 complex than from the wild type counterparts. Activity measurements, gel filtration, and subunit interchange experiments show that the α subunit dissociates more readily from the K87T β2 subunit than from the wild type β2 subunit. The reaction of L-serine to form an external aldimine with Pyridoxal Phosphate at the active site of the K87T β2 subunit markedly increases the affinity for the α subunit and slows removal of Pyridoxal Phosphate by dialysis. We propose that the external aldimine between L-serine and Pyridoxal Phosphate bridges the N-domain and the C-domain in the K87T β2 subunit. This interdomain bridge may mimic the internal aldimine bond in the wild type β2 subunit and stabilize Pyridoxal Phosphate binding. The interdomain bridges formed by the internal aldimine with the wild type β2 subunit and by the external aldimine with L-serine in the K87T β2 subunit may further stabilize interaction with the α subunit because the α/β interaction site contains residues from both N- and C-domains of the β2 subunit.
Sook Shin - One of the best experts on this subject based on the ideXlab platform.
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Pyridoxal Phosphate inhibits the group I intron splicing
Molecular and Cellular Biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene ( td ). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg^2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg^2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K _i of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K _m and decreases in V _max values. (Mol Cell Biochem xxx: 17–34, 2005)
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Pyridoxal Phosphate inhibits the group I intron splicing.
Molecular and cellular biochemistry, 2005Co-Authors: Chul Jung, Sook Shin, In Kook ParkAbstract:The coenzyme Pyridoxal Phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene (td). Of all compounds examined, the Pyridoxal Phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: Pyridoxal Phosphate > Pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg2+ concentration up to 14 mM overcame the suppression of self-splicing by Pyridoxal Phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg2+. The kinetic analysis demonstrated that Pyridoxal Phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a K(i) of 11.8 mM. The specificity of the splicing inhibition by Pyridoxal Phosphate is predominantly due to increases in K(m) and decreases in V(max) values.
Otto Ristau - One of the best experts on this subject based on the ideXlab platform.
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Pyridoxal Phosphate induced association reactions of adrenodoxin and adrenodoxin-reductase.
Biochemical and biophysical research communications, 1996Co-Authors: Joachim Behlke, Otto RistauAbstract:Pyridoxal Phosphate, cofactor of several enzymes, possesses linking properties to induce oligomerization of identical proteins such as adrenodoxin-reductase or adrenodoxin. The capability to get such self-assemblies is slightly lower than that for obtaining the heterologous complex between adrenodoxin-reductase and adrenodoxin which was found to be essential for electron transfer in the cytochrome P450 system. The influence of Pyridoxal Phosphate on the complex formation between adrenodoxin-reductase and adrenodoxin as well as the oligomerization reaction of the isolated proteins and possible consequences is discussed.
