The mechanism of action of glyceraldehyde-3-phosphate dehydrogenase

Polgár, László

doi:10.1007/bf02147997

Experientia

1964

DOI: 10.1007/bf02147997

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The mechanism of action of glyceraldehyde-3-phosphate dehydrogenase

László Polgár

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1967

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Cited by 21 publications

(2 citation statements)

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“…GAPDH is a glycolytic enzyme involved in bacterial energy generation that is essential for growth in the absence of neoglucogenic substrates (26,27). In several pathogenic bacteria, GAPDH has been described as a protein associated with virulence (28 -30) due to its ability to bind several host proteins (28,(31)(32)(33) or to confer resistance against reactive oxygen species produced by host phagocytic cells (34).…”

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confidence: 99%

Streptococcus agalactiae GAPDH Is a Virulence-Associated Immunomodulatory Protein

Madureira¹,

Baptista

Vieira

et al. 2007

The Journal of Immunology

127

109

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Certain extracellular proteins produced by several pathogenic microorganisms interfere with the host immune system facilitating microbial colonization and were thus designated virulence-associated immunomodulatory proteins. In this study, a protein with B lymphocyte stimulatory activity was isolated from culture supernatants of Streptococcus agalactiae strain NEM316. This protein, with an apparent molecular mass of 45 kDa, was identified as GAPDH by N-terminal amino acid sequencing. The gapC gene was cloned and expressed in Escherichia coli for the production of a recombinant histidyl-tagged protein. The recombinant GAPDH (rGAPDH), purified in an enzymatically active form, induced in vitro an up-regulation of CD69 expression on B cells from normal and BCR transgenic mice. In addition, rGAPDH induced an increase in the numbers of total, but not of rGAPDH-specific, splenic Ig-secreting cells in C57BL/6 mice treated i.p. with this protein. These in vitro- and in vivo-elicited B cell responses suggest that the B cell stimulatory effect of rGAPDH is independent of BCR specificity. A S. agalactiae strain overexpressing GAPDH showed increased virulence as compared with the wild-type strain in C57BL/6 mice. This virulence was markedly reduced in IL-10-deficient and anti-rGAPDH antiserum-treated mice. These results suggest that IL-10 production, which was detected at higher concentrations in the serum of rGAPDH-treated mice, is important in determining the successfulness of the host colonization by S. agalactiae and they highlight the direct role of GAPDH in this process. Taken together, our data demonstrate that S. agalactiae GAPDH is a virulence-associated immunomodulatory protein.

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mentioning

confidence: 99%

Streptococcus agalactiae GAPDH Is a Virulence-Associated Immunomodulatory Protein

Madureira¹,

Baptista

Vieira

et al. 2007

The Journal of Immunology

127

109

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“…In living organisms, phosphorylation and dephosphorylation are required for energy storage/release, enzyme activation/deactivation, and catabolism. − Many kinases and phosphatases are involved in these reactions. Because dephosphorylation by alkaline phosphatase (ALP) is very fast, ALP is commonly used as a catalytic label in biosensors. − Some redox enzymes, such as dehydrogenases, can also be involved in the reversible oxidative phosphorylation, using NAD + as an oxidant. − Its reverse reaction corresponds to the reductive dephosphorylation using NADH as a reductant. NAD(P)H dehydrogenase (quinone) [DT-diaphorase (DT-D)] is a redox enzyme that catalyzes the two-electron reduction of quinones by using NADH or NADPH as a reductant.…”

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Use of a Phosphatase-Like DT-Diaphorase Label for the Detection of Outer Membrane Vesicles

et al. 2019

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DT-diaphorase (DT-D) is known to mainly catalyze the two-electron reduction of quinones and nitro(so) compounds. Detection of Gram-negative bacterial outer membrane vesicles (OMVs) that contain pyrogenic lipopolysaccharides (LPSs, also called endotoxins) is required for evaluating the toxic effects of analytical samples. Here, we report that DT-D has a high dephosphorylation activity: DT-D catalyzes reductive dephosphorylation of a phosphate-containing substrate in the presence of NADH. We also report that sensitive and simple OMV detection is possible with a sandwich-type electrochemical immunosensor using DT-D and two identical LPS-binding antibodies as a catalytic label and two sandwich probes, respectively. The absorbance change in a solution containing 4-nitrophenyl phosphate indicates that dephosphorylation occurs in the presence of both DT-D and NADH. Among the three phosphate-containing substrates [4-aminophenyl phosphate, ascorbic acid phosphate, and 1-amino-2-naphthyl phosphate (ANP)] that can be converted into electrochemically active products after dephosphorylation, ANP shows the highest electrochemical signal-to-background ratio, because (i) the dephosphorylation of ANP by DT-D is fast, (ii) the electrochemical oxidation of the dephosphorylated product (1-amino-2-naphthol, AN) is rapid, even at a bare indium–tin oxide electrode, and (iii) two redox cycling processes significantly increase the electrochemical signal. The two redox cycling processes include an electrochemical–enzymatic redox cycling and an electrochemical–chemical redox cycling. The electrochemical signal in a neutral buffer (tris buffer, pH 7.5) is comparable to that in a basic buffer (tris buffer, pH 9.5). When the immunosensor is applied to the detection of OMV from Escherichia coli, the detection limit is found to be 8 ng/mL. This detection strategy is highly promising for the detection of biomaterials, including other extracellular vesicles.

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Simultaneous binding of coenzyme-competitive inhibitors of yeast alcohol dehydrogenase

Fonda

Anderson

1967

Archives of Biochemistry and Biophysics

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The mechanism of action of glyceraldehyde-3-phosphate dehydrogenase

Cited by 21 publications

References 28 publications

Streptococcus agalactiae GAPDH Is a Virulence-Associated Immunomodulatory Protein

Streptococcus agalactiae GAPDH Is a Virulence-Associated Immunomodulatory Protein

Use of a Phosphatase-Like DT-Diaphorase Label for the Detection of Outer Membrane Vesicles

Simultaneous binding of coenzyme-competitive inhibitors of yeast alcohol dehydrogenase

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