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Chemical Compound Review

Benzoylformate     2-oxo-2-phenyl-ethanoic acid

Synonyms: CHEMBL950, SureCN38943, AC-105, B13055_ALDRICH, AG-G-22626, ...
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Disease relevance of alpha-Oxobenzeneacetic acid


High impact information on alpha-Oxobenzeneacetic acid


Chemical compound and disease context of alpha-Oxobenzeneacetic acid


Biological context of alpha-Oxobenzeneacetic acid


Anatomical context of alpha-Oxobenzeneacetic acid


Associations of alpha-Oxobenzeneacetic acid with other chemical compounds


Gene context of alpha-Oxobenzeneacetic acid

  • Each day, the following urinary metabolites were analysed from samples collected during exposure (0-6 h) and after exposure (6-24 h): mandelic acid; phenylglyoxylic acid; and two mercapturic acids, N-acetyl-S-(1-phenyl-2-hydroxyethyl)-L-cysteine (M1) and N-acetyl-S-(2-phenyl-2-hydroxyethyl)-L-cysteine (M2) [22].
  • Examination of growth curves and patterns of substrate utilization, as well as measurement of enzyme activities, showed that benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II are repressed when A. calcoaceticus utilizes L-mandelate or phenylglyoxylate [23].

Analytical, diagnostic and therapeutic context of alpha-Oxobenzeneacetic acid


  1. Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism. Dewanti, A.R., Xu, Y., Mitra, B. Biochemistry (2004) [Pubmed]
  2. Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Tsou, A.Y., Ransom, S.C., Gerlt, J.A., Buechter, D.D., Babbitt, P.C., Kenyon, G.L. Biochemistry (1990) [Pubmed]
  3. Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase. Wang, J., Golbik, R., Seliger, B., Spinka, M., Tittmann, K., Hübner, G., Jordan, F. Biochemistry (2001) [Pubmed]
  4. Phenylacetyl-CoA:acceptor oxidoreductase, a new alpha-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Schneider, S., Fuchs, G. Arch. Microbiol. (1998) [Pubmed]
  5. Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii. Hirsch, W., Schägger, H., Fuchs, G. Eur. J. Biochem. (1998) [Pubmed]
  6. Accelerating unimolecular decarboxylation by preassociated Acid catalysis in thiamin-derived intermediates: implicating br??nsted acids as carbanion traps in enzymes. Kluger, R., Ikeda, G., Hu, Q., Cao, P., Drewry, J. J. Am. Chem. Soc. (2006) [Pubmed]
  7. Review of the metabolic fate of styrene. Sumner, S.J., Fennell, T.R. Crit. Rev. Toxicol. (1994) [Pubmed]
  8. Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on wild-type indolepyruvate decarboxylase and variants using indolepyruvate, benzoylformate, and pyruvate as substrates. Schütz, A., Golbik, R., König, S., Hübner, G., Tittmann, K. Biochemistry (2005) [Pubmed]
  9. Steady-state kinetics and molecular evolution of Escherichia coli MenD [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase], an anomalous thiamin diphosphate-dependent decarboxylase-carboligase. Bhasin, M., Billinsky, J.L., Palmer, D.R. Biochemistry (2003) [Pubmed]
  10. Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues. Weiss, P.M., Garcia, G.A., Kenyon, G.L., Cleland, W.W., Cook, P.F. Biochemistry (1988) [Pubmed]
  11. A methyl-accepting protein is involved in benzoate taxis in Pseudomonas putida. Harwood, C.S. J. Bacteriol. (1989) [Pubmed]
  12. Acyloin formation by benzoylformate decarboxylase from Pseudomonas putida. Wilcocks, R., Ward, O.P., Collins, S., Dewdney, N.J., Hong, Y., Prosen, E. Appl. Environ. Microbiol. (1992) [Pubmed]
  13. Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase. Knoll, M., M??ller, M., Pleiss, J., Pohl, M. Chembiochem (2006) [Pubmed]
  14. Benzoylformate decarboxylase from Pseudomonas putida as stable catalyst for the synthesis of chiral 2-hydroxy ketones. Iding, H., Dünnwald, T., Greiner, L., Liese, A., Müller, M., Siegert, P., Grötzinger, J., Demir, A.S., Pohl, M. Chemistry (Weinheim an der Bergstrasse, Germany) (2000) [Pubmed]
  15. Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution. Lingen, B., Kolter-Jung, D., Dünkelmann, P., Feldmann, R., Grötzinger, J., Pohl, M., Müller, M. Chembiochem (2003) [Pubmed]
  16. Excretion of N-acetyl-S-(1-phenyl-2-hydroxyethyl)-cysteine and N-acetyl-S-(2-phenyl-2-hydroxyethyl)-cysteine in workers exposed to styrene. Maestri, L., Imbriani, M., Ghittori, S., Capodaglio, E., Gobba, F., Cavalleri, A. Sci. Total Environ. (1997) [Pubmed]
  17. Microdetermination of 2-ketoglutaric acid in plasma and cerebrospinal fluid by capillary gas chromatography mass spectrometry; application to pediatrics. Rocchiccioli, F., Leroux, J.P., Cartier, P.H. Biomed. Mass Spectrom. (1984) [Pubmed]
  18. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Polovnikova, E.S., McLeish, M.J., Sergienko, E.A., Burgner, J.T., Anderson, N.L., Bera, A.K., Jordan, F., Kenyon, G.L., Hasson, M.S. Biochemistry (2003) [Pubmed]
  19. L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain. Illias, R.M., Sinclair, R., Robertson, D., Neu, A., Chapman, S.K., Reid, G.A. Biochem. J. (1998) [Pubmed]
  20. Purification and crystallization of benzoylformate decarboxylase. Hasson, M.S., Muscate, A., Henehan, G.T., Guidinger, P.F., Petsko, G.A., Ringe, D., Kenyon, G.L. Protein Sci. (1995) [Pubmed]
  21. Modified substrate specificity of L-hydroxyisocaproate dehydrogenase derived from structure-based protein engineering. Feil, I.K., Hendle, J., Schomburg, D. Protein Eng. (1997) [Pubmed]
  22. Urinary excretion of mandelic, phenylglyoxylic, and specific mercapturic acids in rats exposed repeatedly by inhalation to various concentrations of styrene vapors. Truchon, G., Gérin, M., Brodeur, J. Can. J. Physiol. Pharmacol. (1990) [Pubmed]
  23. Regulation of growth of Acinetobacter calcoaceticus NCIB8250 on benzyl alcohol in batch culture. Beggs, J.D., Cook, A.M., Fewson, C.A. J. Gen. Microbiol. (1976) [Pubmed]
  24. Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis. Lingen, B., Grötzinger, J., Kolter, D., Kula, M.R., Pohl, M. Protein Eng. (2002) [Pubmed]
  25. Enantioseparation by HPLC using phenylcarbonate, benzoylformate, p-toluenesulfonylcarbamate, and benzoylcarbamates of cellulose and amylose as chiral stationary phases. Ikai, T., Yamamoto, C., Kamigaito, M., Okamoto, Y. Chirality. (2005) [Pubmed]
  26. Exposure-excretion relationship of styrene and acetone in factory workers: a comparison of a lipophilic solvent and a hydrophilic solvent. Mizunuma, K., Yasugi, T., Kawai, T., Horiguchi, S., Ikeda, M. Arch. Environ. Contam. Toxicol. (1993) [Pubmed]
  27. Construction of an electro-enzymatic bioreactor for the production of (R)-mandelate from benzoylformate. Kim, M.H., Yun, S.E. Biotechnol. Lett. (2004) [Pubmed]
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