Inactivation of phosphofructokinase by dialdehyde-ATP

Gregory, Martha R.; Kaiser, E.

doi:10.1016/0003-9861(79)90567-8

Cited by 31 publications

(14 citation statements)

References 43 publications

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“…[14CloATP was found to radiolabel protein, whereas t3*P]oATP did not (Lowe et al, 1979). Modification with oATP has been found to be stabilized by the presence of borate, indicating the presence of a diol (Gregory & Kaiser, 1979). A second mechanism for modification by oATP has been proposed that involves both aldehyde groups of oATP and removal of the triphosphate moiety producing a dihydroxymorpholino derivative ( Fig.…”

Section: Adduct Formationmentioning

confidence: 99%

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ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway

Craig

Wallace

1993

Protein Science

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Eukaryotic cytochrome c possesses an ATP-binding site of substantial specificity and high affinity that is conserved between highly divergent species and which includes the invariant residue arginine''. Such evolutionary conservatism strongly suggests a physiological role for ATP binding that demands further investigation. We report the preparation of adducts of the protein and the affinity labels 8-azido adenosine 5'-triphosphate, adenosine S-triphosphate-T,3'-diaIdehyde, and 5'-p-fluorosulfonylbenzoyladenosine. The two former reagents were seen to react at the arginine9'-containing site, yet the reaction of the latter, although specific, occurred elsewhere, suggesting caution is necessary in its use. None of the adducts displayed significant modification of global structure, stability, or physicochemical properties, leading us to believe that the 8-N3-ATP and oATP adducts are good stabilized models of the noncovalent interaction; yet modification led to significant, and sometimes pronounced, effects on biological activity. We therefore propose that the role of ATP binding to this site, which we have shown to occur when the phosphorylation potential of the system is high under the equivalent of physiological conditions, is to cause a decrease in electron flow through the mitochondrial electron transport chain. Differences in the degree of inhibition produced by differences in adduct chemistry suggest that this putative regulatory role is mediated primarily by electrostatic effects.

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Section: Adduct Formationmentioning

confidence: 99%

“…Reaction of oATP with lysine residues. The reaction of a lysine residue with oATP, as proposed byGregory and Kaiser (1979) andKing and Colman (1983), is shown.…”

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confidence: 91%

ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway

Craig

Wallace

1993

Protein Science

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“…These methods are often limited by poor efficiency of cross-linking to polymerases. Another modification, periodate-oxidized NTPs, provides excellent cross-linking efficiency which has been demonstrated for other classes of proteins (Clertant & Cuzin, 1982;Esterbrook-Smith et al, 1976;Gregory & Kaiser, 1979;Lowe & Beechey, 1982; King & Colman, 1983). This method has been employed in the studies described in this report to explore the nucleotide binding site(s) in poliovirus RNA polymerase (3DP01).…”

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confidence: 99%

Identification of nucleotide binding sites in the poliovirus RNA polymerase

Richards

Hanson²,

Schultz³

et al. 1995

Biochemistry

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Poliovirus RNA polymerase (3Dpol) was cross-linked to [32P]ribonucleoside triphosphates (NTPs) by reduction of oxidized NTP-protein complexes. Cross-linked complexes were digested with cyanogen bromide, and resulting peptides were fractionated by reverse-phase HPLC. 32P-Labeled peptides were purified by secondary HPLC fractionation and/or additional digestion with endoproteinases Glu-C, TPCK-trypsin, or Asp-N followed by another HPLC fractionation. N-Terminal sequences of the major [32P]-peptides were determined, and approximate sizes of these peptides were obtained by SDS-polyacrylamide gel electrophoresis. Two major NTP binding sites in 3Dpol were found. One site was between Asp-266 and Met-286; possible binding residues in this fragment were Lys-276, Lys-278, or Lys-283. A second binding site was between Ala-57 and Met-74 with Lys-61 or Lys-66 as possible binding residues. Alignment of these regions on the known structure of HIV-1 reverse transcriptase allowed us to predict the position of the downstream nucleotide binding site in the conserved "fingers" subdomain present near the active site cleft of both RNA and DNA polymerases. The N-terminal nucleotide binding site is not contained within a region that is conserved among other polymerases.

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“…Clearly, oCTP and not contaminating anhydro-oC are responsible for most of the inactivation. Others have demonstrated this type of enzyme accelerated b-elimination reaction with radioactively labeled dialdehyde nucleotides~Lowe & Beechey, 1982; King & Colman, 1983!. Some studies using periodate oxidized nucleotides have provided evidence that the covalent modification proceeds by formation of a Schiff base while others have indicated that a morpholino structure is formed~Hansske et al, 1974; Gregory & Kaiser, 1979;Lowe & Beechey, 1982;King & Colman, 1983, 1990Mas & Colman, 1983;Rayford et al, 1985;White & Levy, 1987;Colman, 1990!. Morpholino derivatives are fairly stable under moderate conditions, but harsher treatment releases or degrades the modifi- peaks at m0z 1,759.8 and 1,761.8 with a single major prompt fragment at m0z 1,650.7.…”

Section: Discussionmentioning

confidence: 99%

“…cation~Gregory & Kaiser, 1979;King & Carlson, 1981! as was the case with the oCTP adduct formed with CMP-NeuAc synthetase.…”

Section: Discussionmentioning

confidence: 99%

Covalent modification of lys19 in the ctp binding site of cytidine 5′‐monophosphate n‐acetylneuraminic acid synthetase

1999

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Periodate oxidized CTP~oCTP! was used to investigate the importance of lysine residues in the CTP binding site of the cytidine 59-monophosphate N-acetylneuraminic acid~CMP-NeuAc! synthetase~EC 2.7.7.43! from Haemophilus ducreyi. The reaction of oCTP with the enzyme follows pseudo-first-order saturation kinetics, giving a maximum rate of inactivation of 0.6 min Ϫ1 and a K I of 6.0 mM at pH 7.1. Mass spectrometric analysis of the modified enzyme provided data that was consistent with b-elimination of triphosphate after the reaction of oCTP with the enzyme. A fully reduced enzyme-oCTP conjugate, retaining the triphosphate moiety, was obtained by inclusion of NaBH 3 CN in the reaction solution. The b-elimination product of oCTP reacted several times more rapidly with the enzyme compared to equivalent concentrations of oCTP. This compound also formed a stable reduced morpholino adduct with CMP-NeuAc synthetase when the reaction was conducted in the presence of NaBH 3 CN, and was found to be a useful lysine modifying reagent. The substrate CTP was capable of protecting the enzyme to a large degree from inactivation by oCTP and its b-elimination product. Lys19, a residue conserved in CMP-NeuAc synthetases, was identified as being labeled with the b-elimination product of oCTP.Keywords: affinity labeling; CMP-NeuAc synthetase; Haemophilus ducreyi; mass spectrometry; periodate oxidized CTP; sialic acid Sialic acids are nine carbon a-keto acid monosaccharides that have many important biological effects, particularly in cellular recognition~Schauer, 1985;Kelm et al., 1996!. Although commonly found in higher animals and present in all mammals, sialic acids have been found in relatively few microorganisms~Schauer et al., 1995!. In bacteria, sialic acid presents as the terminal residue of lipooligosaccharides~LOS! and in the form of polymeric extracellular capsules is capable of masking surface epitopes and inhibiting phagocytosis of the bacteria~Timmis et al., 1985;Parsons et al., 1988;Rest & Frangipane, 1992!. Haemophilus ducreyi is the Gram-negative bacterium that is the causative agent of the sexually transmitted disease chancroid. Chancroid is common in Africa, Asia, and Latin America. Although the incidence of cases in the United States is low, outbreaks have occurred in recent years~Trees & Morse, 1995!. In addition, the incidence of the disease may be greater than previously estimated Webb et al., 1995!. The LOS of H. ducreyi has been determined to be a virulence factor~Odumeru et al., 1987;Campagnari et al., 1991;Lagergard, 1992!. Furthermore, the LOS from H. ducreyi, along with other Haemophilus and Neisseria spp., are structurally similar to the carbohydrates of some human glycolipids and glycoproteins~Campagnari et al ., 1990;Mandrell & Apicella, 1993!. It has been hypothesized that this mimicry may allow the organism to evade host immune defenses and utilize host receptors for adherence. Sialic acid has recently been identified as a major component of the LOS from many strains of H. ducreyi, yet the preci...

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Inactivation of phosphofructokinase by dialdehyde-ATP

Cited by 31 publications

References 43 publications

ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway

ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway

Identification of nucleotide binding sites in the poliovirus RNA polymerase

Covalent modification of lys19 in the ctp binding site of cytidine 5′‐monophosphate n‐acetylneuraminic acid synthetase

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