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Chemical Compound Review

phenylglyoxal     2-oxo-2-phenyl-ethanal

Synonyms: CCRIS 966, CHEMBL233632, ACMC-1BYN2, LS-447, Phenyl glyoxal, ...
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Disease relevance of phenylglyoxal

  • Chemical modification of adenylosuccinate synthetase from Escherichia coli with phenylglyoxal resulted in an inhibition of enzyme activity with a second-order rate constant of 13.6 M-1 min-1 [1].
  • Incubation of the exocellular DD-carboxypeptidase/transpeptidase of Streptomyces R61 with phenylglyoxal resulted in a time-dependent decrease in the enzyme activity [2].
  • Phenylglyoxal rapidly and completely inactivates spinach and Rhodospirillum rubrum ribulosebisphosphate carboxylases [3].
  • Comparative analysis of the cytotoxicity of substituted [phenylglyoxal bis(4-methyl-3-thiosemicarbazone)] copper(II) chelates. 2. Parabolic correlations and their implications for selective toxicity [4].
  • Seven para-substituted [phenylglyoxal bis(4-methyl-3-thiosemicarbazone)]copper (II) chelates (12-18) have been designed, synthesized, and tested for their ability to inhibit the respiration of rat liver slices as a normal cell model and Ehrlich ascites cells as a tumor cell model [5].

High impact information on phenylglyoxal


Chemical compound and disease context of phenylglyoxal


Biological context of phenylglyoxal


Anatomical context of phenylglyoxal

  • Treatment of the plasma membrane H+-ATPase of Neurospora crassa with the arginine-specific reagents phenylglyoxal or 2,3-butanedione at 30 degrees C, pH 7.0, leads to a marked inhibition of ATPase activity [18].
  • In contrast, the activity of terminal deoxynucleotidyl-transferase, a template-independent DNA polymerase isolated from calf thymus, is not inhibited by phenylglyoxal [19].
  • Treatment of the partially purified lymphocyte activating factor with phenylglyoxal reduced the thymocyte-stimulating activity 99% and the chondrocyte-stimulating activity 100% [20].
  • Effects of the arginyl- and lysyl-specific reagent phenylglyoxal (PGO) on the epithelial Na+ channel were evaluated by measuring the amiloride-blockable 22Na+ fluxes in membrane vesicles derived from the toad bladder epithelium [21].
  • Isolated rat liver mitochondria were treated with the arginine-specific chemical reagent 2, 3-butanedione or phenylglyoxal, followed by removal of excess free reagent [22].

Associations of phenylglyoxal with other chemical compounds


Gene context of phenylglyoxal


Analytical, diagnostic and therapeutic context of phenylglyoxal

  • However, protection by substrates was achieved only after treatment with phenylglyoxal [33].
  • The labeled phenylglyoxal-treated enzyme was digested with trypsin, and the radiolabeled peptides were purified by high-performance liquid chromatography on reversed-phase columns [34].
  • The phenylglyoxal-modified peptide was isolated by a procedure involving limited digestion by trypsin, separation of the tryptic peptides by high pressure liquid chromatography (HPLC), further digestion of the modified peptide by pepsin, and a final purification by HPLC [35].
  • Sequence analysis of tryptic peptides indicated that Arg147 is the site of phenylglyoxal chemical modification [1].
  • A detailed analysis of the inhibitory process carried out using avian myeloblastosis virus (AMV) DNA polymerase as a test enzyme revealed that inclusion of template-primer during the preincubation with phenylglyoxal, but not substrate triphosphates or primer alone, protects the enzyme against phenylglyoxal inactivation [19].


  1. Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis. Dong, Q., Liu, F., Myers, A.M., Fromm, H.J. J. Biol. Chem. (1991) [Pubmed]
  2. Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase. Bourguignon-Bellefroid, C., Joris, B., Van Beeumen, J., Ghuysen, J.M., Frère, J.M. Biochem. J. (1992) [Pubmed]
  3. Inactivation of ribulosebisphosphate carboxylase by modification of arginyl residues with phenylglyoxal. Schloss, J.V., Norton, I.L., Stringer, C.D., Hartman, F.C. Biochemistry (1978) [Pubmed]
  4. Comparative analysis of the cytotoxicity of substituted [phenylglyoxal bis(4-methyl-3-thiosemicarbazone)] copper(II) chelates. 2. Parabolic correlations and their implications for selective toxicity. Coats, E.A., Milstein, S.R., Pleiss, M.A., Roesener, J.A. J. Med. Chem. (1978) [Pubmed]
  5. Comparative analysis of the cytotoxicity of substituted (phenylglyoxal bis(4-methyl-3-thiosemicarbazone)) copper (II) chelates. Coats, E.A., Milstein, S.R., Holbein, G., McDonald, J., Reed, R., Petering, H.G. J. Med. Chem. (1976) [Pubmed]
  6. Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Garrett, R.M., Johnson, J.L., Graf, T.N., Feigenbaum, A., Rajagopalan, K.V. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. Reconstitution of purified brown adipose tissue mitochondria uncoupling protein: demonstration of separate identity of nucleotide binding and proton translocation sites by chemical probes. Katiyar, S.S., Shrago, E. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  8. Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase. Mautner, H.G., Pakula, A.A., Merrill, R.E. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  9. Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands. Johans, M., Milanesi, E., Franck, M., Johans, C., Liobikas, J., Panagiotaki, M., Greci, L., Principato, G., Kinnunen, P.K., Bernardi, P., Costantini, P., Eriksson, O. J. Biol. Chem. (2005) [Pubmed]
  10. Essential arginine residues in tryptophanase from Escherichia coli. Kazarinoff, M.N., Snell, E.E. J. Biol. Chem. (1977) [Pubmed]
  11. Kinetics of the inactivation of Escherichia coli glutamate apodecarboxylase by phenylglyoxal. Cheung, S.T., Fonda, M.L. Arch. Biochem. Biophys. (1979) [Pubmed]
  12. Implication of arginyl residues in mRNA binding to ribosomes. Hernández, F., López-Rivas, A., Pintor-Toro, J.A., Vázquez, D., Palacián, E. Eur. J. Biochem. (1980) [Pubmed]
  13. Inactivation of Escherichia coli 2-amino-3-ketobutyrate CoA ligase by phenylglyoxal and identification of an active-site arginine peptide. Mukherjee, J.J., Dekker, E.E. Arch. Biochem. Biophys. (1992) [Pubmed]
  14. Evidence that chemical modification of a positively charged residue at position 189 causes the loss of catalytic activity of iron-containing and manganese-containing superoxide dismutases. Chan, V.W., Bjerrum, M.J., Borders, C.L. Arch. Biochem. Biophys. (1990) [Pubmed]
  15. Chemical modification of arginine residues of rat liver S-adenosylhomocysteinase. Takata, Y., Fujioka, M. J. Biol. Chem. (1983) [Pubmed]
  16. An essential residue at the active site of aspartate transcarbamylase. Kantrowitz, E.R., Lipscomb, W.N. J. Biol. Chem. (1976) [Pubmed]
  17. Phenylglyoxal is not a selective inhibitor of phagocytosis. van Schaik, M.L., Weening, R.S., Roos, D. J. Cell. Sci. (1979) [Pubmed]
  18. Characterization of an essential arginine residue in the plasma membrane H+-ATPase of Neurospora crassa. Kasher, J.S., Allen, K.E., Kasamo, K., Slayman, C.W. J. Biol. Chem. (1986) [Pubmed]
  19. Phenylglyoxal as a template site-specific reagent for DNA and RNA polymerases. Selective inhibition of initiation. Srivastava, A., Modak, M.J. J. Biol. Chem. (1980) [Pubmed]
  20. In vitro activation of human chondrocytes and synoviocytes by a human interleukin-1-like factor. McGuire-Goldring, M.B., Meats, J.E., Wood, D.D., Ihrie, E.J., Ebsworth, N.M., Russell, R.G. Arthritis Rheum. (1984) [Pubmed]
  21. Sodium-dependent inhibition of the epithelial sodium channel by an arginyl-specific reagent. Garty, H., Yeger, O., Asher, C. J. Biol. Chem. (1988) [Pubmed]
  22. Chemical modification of arginines by 2,3-butanedione and phenylglyoxal causes closure of the mitochondrial permeability transition pore. Eriksson, O., Fontaine, E., Bernardi, P. J. Biol. Chem. (1998) [Pubmed]
  23. Ligand-selective modulation of the permeability transition pore by arginine modification. Opposing effects of p-hydroxyphenylglyoxal and phenylglyoxal. Linder, M.D., Morkunaite-Haimi, S., Kinnunen, P.K., Bernardi, P., Eriksson, O. J. Biol. Chem. (2002) [Pubmed]
  24. A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney. Davidson, W.S., Flynn, T.G. J. Biol. Chem. (1979) [Pubmed]
  25. Functionally important arginine residues of aspartate transcarbamylase. Kantrowitz, E.R., Lipscomb, W.N. J. Biol. Chem. (1977) [Pubmed]
  26. An essential arginine residue at the substrate-binding site of p-hydroxybenzoate hydroxylase. Shoun, H., Beppu, T., Arima, K. J. Biol. Chem. (1980) [Pubmed]
  27. Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents. Horowitz, P.M., Bowman, S. J. Biol. Chem. (1987) [Pubmed]
  28. Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae. Furneisen, J.M., Carman, G.M. Biochim. Biophys. Acta (2000) [Pubmed]
  29. The role of arginine residues in interleukin 1 receptor binding. Nanduri, V.B., Hulmes, J.D., Pan, Y.C., Kilian, P.L., Stern, A.S. Biochim. Biophys. Acta (1991) [Pubmed]
  30. Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal. Weng, L., Heinrikson, R.L., Westley, J. J. Biol. Chem. (1978) [Pubmed]
  31. Active site labelling of inositol 1,4,5-trisphosphate 3-kinase A by phenylglyoxal. Communi, D., Lecocq, R., Vanweyenberg, V., Erneux, C. Biochem. J. (1995) [Pubmed]
  32. Chemical modification of an arginine residue in aldose reductase is enhanced by coenzyme binding: further evidence for conformational change during the reaction mechanism. Flynn, T.G., Kubiseski, T.J. Adv. Enzyme Regul. (1993) [Pubmed]
  33. Functional reconstitution of the lysosomal sialic acid carrier into proteoliposomes. Mancini, G.M., Beerens, C.E., Galjaard, H., Verheijen, F.W. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  34. Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase. Usha, R., Savithri, H.S., Rao, N.A. J. Biol. Chem. (1992) [Pubmed]
  35. Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant. Bateman, R.C., Jackson, D., Slaughter, C.A., Unnithan, S., Chai, Y.G., Moomaw, C., Hersh, L.B. J. Biol. Chem. (1989) [Pubmed]
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