Chemical Compound Review:
phenylglyoxal 2-oxo-2-phenyl-ethanal
Synonyms:
CCRIS 966, CHEMBL233632, ACMC-1BYN2, LS-447, Phenyl glyoxal, ...
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- Essential arginine residues in tryptophanase from Escherichia coli. Kazarinoff, M.N., Snell, E.E. J. Biol. Chem. (1977)
- Kinetics of the inactivation of Escherichia coli glutamate apodecarboxylase by phenylglyoxal. Cheung, S.T., Fonda, M.L. Arch. Biochem. Biophys. (1979)
- 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)
- 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)
- 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)
- Chemical modification of arginine residues of rat liver S-adenosylhomocysteinase. Takata, Y., Fujioka, M. J. Biol. Chem. (1983)
- An essential residue at the active site of aspartate transcarbamylase. Kantrowitz, E.R., Lipscomb, W.N. J. Biol. Chem. (1976)
- Phenylglyoxal is not a selective inhibitor of phagocytosis. van Schaik, M.L., Weening, R.S., Roos, D. J. Cell. Sci. (1979)
- 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)
- 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)
- 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)
- Sodium-dependent inhibition of the epithelial sodium channel by an arginyl-specific reagent. Garty, H., Yeger, O., Asher, C. J. Biol. Chem. (1988)
- 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)
- 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)
- A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney. Davidson, W.S., Flynn, T.G. J. Biol. Chem. (1979)
- Functionally important arginine residues of aspartate transcarbamylase. Kantrowitz, E.R., Lipscomb, W.N. J. Biol. Chem. (1977)
- An essential arginine residue at the substrate-binding site of p-hydroxybenzoate hydroxylase. Shoun, H., Beppu, T., Arima, K. J. Biol. Chem. (1980)
- Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents. Horowitz, P.M., Bowman, S. J. Biol. Chem. (1987)
- Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae. Furneisen, J.M., Carman, G.M. Biochim. Biophys. Acta (2000)
- 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)
- 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)
- 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)
- 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)
- 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)
- Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase. Usha, R., Savithri, H.S., Rao, N.A. J. Biol. Chem. (1992)
- 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)