메뉴 건너뛰기




Volumn 156, Issue 2, 1996, Pages 117-124

Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase

Author keywords

Alcohol dehydrogenase; Aldehyde reductase; Escherichia coli; Methylglyoxal

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE REDUCTASE; METHYLGLYOXAL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0029872670     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00426333     Document Type: Article
Times cited : (42)

References (27)
  • 1
    • 0021195497 scopus 로고
    • Metabolism of methylglyoxal in microorganisms
    • Cooper RA: Metabolism of methylglyoxal in microorganisms. Annu Rev Microbiol 38: 49-68, 1984
    • (1984) Annu Rev Microbiol , vol.38 , pp. 49-68
    • Cooper, R.A.1
  • 2
    • 0023644772 scopus 로고
    • Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone
    • Ray M, Ray S: Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone. J Biol Chem 262: 5974-5977, 1987
    • (1987) J Biol Chem , vol.262 , pp. 5974-5977
    • Ray, M.1    Ray, S.2
  • 3
    • 0025298551 scopus 로고
    • The glyoxalase system: Developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thomalley PJ: The glyoxalase system: developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem J 269: 1-11, 1990
    • (1990) Biochem J , vol.269 , pp. 1-11
    • Thomalley, P.J.1
  • 4
    • 0028276215 scopus 로고
    • Methylglyoxal toxicity in mammals
    • Kalapos MP: Methylglyoxal toxicity in mammals. Toxicol Lett 73: 3-24, 1994
    • (1994) Toxicol Lett , vol.73 , pp. 3-24
    • Kalapos, M.P.1
  • 5
    • 0028181753 scopus 로고
    • Carbon sources for D-lactate formation in rat liver
    • Kondoh Y, Kawase M, Hirata M, Ohmori S: Carbon sources for D-lactate formation in rat liver. J Bio Chem 115: 590-595, 1994
    • (1994) J Bio Chem , vol.115 , pp. 590-595
    • Kondoh, Y.1    Kawase, M.2    Hirata, M.3    Ohmori, S.4
  • 6
    • 0019888193 scopus 로고
    • Isolation of methylglyoxal synthase from goat liver
    • Ray S, Ray M: Isolation of methylglyoxal synthase from goat liver. J Biol Chem 256: 6230-6233, 1981
    • (1981) J Biol Chem , vol.256 , pp. 6230-6233
    • Ray, S.1    Ray, M.2
  • 7
    • 0020491182 scopus 로고
    • Purification and characterization of NAD and NADP-linked α-ketoaldehyde dehydrogenase involved in catalyzing the oxidation of methylglyoxal to pyruvate
    • Ray S, Ray M: Purification and characterization of NAD and NADP-linked α-ketoaldehyde dehydrogenase involved in catalyzing the oxidation of methylglyoxal to pyruvate. J Biol Chem 257: 10566-10570, 1982
    • (1982) J Biol Chem , vol.257 , pp. 10566-10570
    • Ray, S.1    Ray, M.2
  • 8
    • 0021684373 scopus 로고
    • Purification and partial characterization of a methylglyoxal reductase from goat liver
    • Ray M, Ray S: Purification and partial characterization of a methylglyoxal reductase from goat liver. Biochim Biophys Acta 802: 119-127, 1984
    • (1984) Biochim Biophys Acta , vol.802 , pp. 119-127
    • Ray, M.1    Ray, S.2
  • 9
    • 0022356242 scopus 로고
    • Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae
    • Murata K, Fukada Y, Simosaka M, Watanabe K, Saikusa T, Kimura A: Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur J Biochem 151: 631-636, 1985
    • (1985) Eur J Biochem , vol.151 , pp. 631-636
    • Murata, K.1    Fukada, Y.2    Simosaka, M.3    Watanabe, K.4    Saikusa, T.5    Kimura, A.6
  • 11
    • 0023040210 scopus 로고
    • Metabolism of 2-oxoaldehydes in yeasts. Possible role of glycolytic bypath as a detoxification system in L-threonine catabolism by Saccharomyces cerevisiae
    • Murata K, Saikusa T, Fukuda Y, Watanabe K, Inoue Y, Shimosaka M, Kimura A: Metabolism of 2-oxoaldehydes in yeasts. Possible role of glycolytic bypath as a detoxification system in L-threonine catabolism by Saccharomyces cerevisiae. Eur J Biochem 157: 297-301, 1986
    • (1986) Eur J Biochem , vol.157 , pp. 297-301
    • Murata, K.1    Saikusa, T.2    Fukuda, Y.3    Watanabe, K.4    Inoue, Y.5    Shimosaka, M.6    Kimura, A.7
  • 12
    • 0023837912 scopus 로고
    • D-Lactate production by Leishmania braziliensis through the glyoxalase pathway
    • Darling TN, Blum JJ: D-Lactate production by Leishmania braziliensis through the glyoxalase pathway. Mol Biochem Parasitol 28: 121-128, 1988
    • (1988) Mol Biochem Parasitol , vol.28 , pp. 121-128
    • Darling, T.N.1    Blum, J.J.2
  • 13
    • 0024399730 scopus 로고
    • Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes
    • Ghoshal K, Banerjee AB, Ray S: Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes. Mol Biochem Parasitol 35: 21-30, 1989
    • (1989) Mol Biochem Parasitol , vol.35 , pp. 21-30
    • Ghoshal, K.1    Banerjee, A.B.2    Ray, S.3
  • 14
    • 0015349185 scopus 로고
    • The purification and properties of Escherichia coli methylglyoxal synthase
    • Hopper DJ, Cooper RA: The purification and properties of Escherichia coli methylglyoxal synthase. Biochem J 128: 321-329, 1972
    • (1972) Biochem J , vol.128 , pp. 321-329
    • Hopper, D.J.1    Cooper, R.A.2
  • 15
    • 0026603415 scopus 로고
    • The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amine oxidase in human umbilical artery
    • Lyles GA, Chalmers J: The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amine oxidase in human umbilical artery. Biochem Pharmacol 43: 1409-1414, 1992
    • (1992) Biochem Pharmacol , vol.43 , pp. 1409-1414
    • Lyles, G.A.1    Chalmers, J.2
  • 17
    • 0001739947 scopus 로고
    • The mechanism of action of glyoxalase
    • Racker E: The mechanism of action of glyoxalase. J Biol Chem 190: 685-696, 1951
    • (1951) J Biol Chem , vol.190 , pp. 685-696
    • Racker, E.1
  • 18
    • 0021722256 scopus 로고
    • Oxidation of lactaldehyde by cytosolic aldehyde dehydrogenase and inhibition of cytosolic and mitochondrial aldehyde dehydrogenase by metabolites
    • Ray S, Ray M: Oxidation of lactaldehyde by cytosolic aldehyde dehydrogenase and inhibition of cytosolic and mitochondrial aldehyde dehydrogenase by metabolites. Biochim Biophys Acta 802: 128-134, 1984
    • (1984) Biochim Biophys Acta , vol.802 , pp. 128-134
    • Ray, S.1    Ray, M.2
  • 20
    • 0018053915 scopus 로고
    • The living state and cancer
    • Szent-Györgyi A: The living state and cancer. Ciba Found Symp 67: 3-18, 1979
    • (1979) Ciba Found Symp , vol.67 , pp. 3-18
    • Szent-Györgyi, A.1
  • 21
    • 0026080404 scopus 로고
    • Inhibition of respiration of tumor cells by methylglyoxal and protection of inhibition by lactaldehyde
    • Ray M, Halder J, Dutta SK, Ray S: Inhibition of respiration of tumor cells by methylglyoxal and protection of inhibition by lactaldehyde. Int J Cancer 47: 603-609, 1991
    • (1991) Int J Cancer , vol.47 , pp. 603-609
    • Ray, M.1    Halder, J.2    Dutta, S.K.3    Ray, S.4
  • 22
    • 0028939260 scopus 로고
    • Glyoxalase III from Escherichia coli: A single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione
    • Misra K, Banerjee AB, Ray S, Ray M: Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem J 305: 999-1003, 1995
    • (1995) Biochem J , vol.305 , pp. 999-1003
    • Misra, K.1    Banerjee, A.B.2    Ray, S.3    Ray, M.4
  • 23
    • 0016414235 scopus 로고
    • Methylglyoxal synthase
    • Cooper RA: Methylglyoxal synthase. Methods Enzymol 41: 502-508, 1975
    • (1975) Methods Enzymol , vol.41 , pp. 502-508
    • Cooper, R.A.1
  • 24
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • Layne E: Spectrophotometric and turbidimetric methods for measuring proteins. Methods Enzymol 3: 447-454, 1957
    • (1957) Methods Enzymol , vol.3 , pp. 447-454
    • Layne, E.1
  • 25
    • 0017406572 scopus 로고
    • Purification and properties of NADPH-dependent aldehyde reductase from human liver
    • Wermuth B, Munch JDB, von Wartburg JP: Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 252: 3821-3828, 1977
    • (1977) J Biol Chem , vol.252 , pp. 3821-3828
    • Wermuth, B.1    Jdb, M.2    Von Wartburg, J.P.3
  • 26
    • 0021111796 scopus 로고
    • Pig muscle aldehyde reductase
    • Cromlish JA, Flynn TG: Pig muscle aldehyde reductase. J Biol Chem 258: 3583-3586, 1983
    • (1983) J Biol Chem , vol.258 , pp. 3583-3586
    • Cromlish, J.A.1    Flynn, T.G.2
  • 27
    • 0017898546 scopus 로고
    • A comparative study of the tissue and species distribution of NADPH-dependent aldehyde reductase
    • Davidson WS, Walton DJ, Flynn TG: A comparative study of the tissue and species distribution of NADPH-dependent aldehyde reductase. Comp Biochem Physiol 60B: 309-315, 1978
    • (1978) Comp Biochem Physiol , vol.60 B , pp. 309-315
    • Davidson, W.S.1    Walton, D.J.2    Flynn, T.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.