메뉴 건너뛰기




Volumn 262, Issue 3, 1999, Pages 704-712

Mechanism of inhibition of aldehyde dehydrogenase by citral, a retinoid antagonist

Author keywords

Aldehyde dehydrogenase; Citral; Enzyme inhibition mechanism; Geranial; Neral

Indexed keywords

ALDEHYDE DEHYDROGENASE; CITRAL; ISOENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RETINOID;

EID: 0033564027     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00415.x     Document Type: Article
Times cited : (56)

References (32)
  • 1
    • 0020488533 scopus 로고
    • Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase
    • 1. Hempel, J.D., Pietruszko, R., Fietzek, P. & Jornvall, H. (1982) Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase. Biochem. USA 21, 6834-6838.
    • (1982) Biochem. USA , vol.21 , pp. 6834-6838
    • Hempel, J.D.1    Pietruszko, R.2    Fietzek, P.3    Jornvall, H.4
  • 2
    • 0025640958 scopus 로고
    • Chemical modification of aldehyde dehydrogenase by a vinyl ketone analog of an insect pheromone
    • 2. Blauer, E.E., Tasayco, M.L., Prestwich, G. & Pietruszko, R. (1990) Chemical modification of aldehyde dehydrogenase by a vinyl ketone analog of an insect pheromone. Biochem. J. 272, 351-358.
    • (1990) Biochem. J. , vol.272 , pp. 351-358
    • Blauer, E.E.1    Tasayco, M.L.2    Prestwich, G.3    Pietruszko, R.4
  • 4
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of alcohol aversion
    • 4. Steinmetz, C.G., Xie, P., Weiner, H. & Hurley, T.D. (1997) Structure of mitochondrial aldehyde dehydrogenase: the genetic component of alcohol aversion. Structure 5, 701-711.
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 5
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • 5. Farrés, J., Wang, T.T.Y., Cunningham, S.J. & Weiner, H. (1995) Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochem. USA 34, 2592-2598.
    • (1995) Biochem. USA , vol.34 , pp. 2592-2598
    • Farrés, J.1    Wang, T.T.Y.2    Cunningham, S.J.3    Weiner, H.4
  • 6
    • 0017406798 scopus 로고
    • Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes
    • 6. Greenfield, N.J. & Pietruszko, R. (1977) Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes. Biochim. Biophys. Acta 483, 35-45.
    • (1977) Biochim. Biophys. Acta , vol.483 , pp. 35-45
    • Greenfield, N.J.1    Pietruszko, R.2
  • 7
    • 0024583015 scopus 로고
    • Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for γ-aminobutyraldehyde
    • 7. Kurys, G., Ambroziak, W. & Pietruszko, R. (1989) Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for γ-aminobutyraldehyde. J. Biol. Chem. 264, 4715-4721.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4715-4721
    • Kurys, G.1    Ambroziak, W.2    Pietruszko, R.3
  • 8
    • 0025785329 scopus 로고
    • Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines and polyamines
    • 8. Ambroziak, W. & Pietruszko, R. (1991) Human aldehyde dehydrogenase: activity with aldehyde metabolites of monoamines, diamines and polyamines. J. Biol. Chem. 266, 13011-13018.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13011-13018
    • Ambroziak, W.1    Pietruszko, R.2
  • 9
    • 0000136523 scopus 로고
    • Biosynthesis of vitamin A with rat intestinal enzymes
    • 9. Goodman, D.S. & Huang, H.S. (1965) Biosynthesis of vitamin A with rat intestinal enzymes. Science 149, 879-880.
    • (1965) Science , vol.149 , pp. 879-880
    • Goodman, D.S.1    Huang, H.S.2
  • 10
    • 0013818626 scopus 로고
    • The enzymatic cleavage of beta-carotene into vitamin A by soluble enzymes of rat liver and intestine
    • 10. Olson, J.A. & Hayaishi, O. (1965) The enzymatic cleavage of beta-carotene into vitamin A by soluble enzymes of rat liver and intestine. Proc. Natl Acad. Sci. USA 54, 1364-1370.
    • (1965) Proc. Natl Acad. Sci. USA , vol.54 , pp. 1364-1370
    • Olson, J.A.1    Hayaishi, O.2
  • 11
    • 0029914087 scopus 로고    scopus 로고
    • β-Oxidation in rabbit liver in vitro and in the perfused ferret liver contributes to retinoic acid biosynthesis from β-apocarotenoic acids
    • 11. Wang, X.-D., Russell, R.M., Liu, C., Stickel, F., Smith, D.E. & Krinsky, N.L. (1996) β-Oxidation in rabbit liver in vitro and in the perfused ferret liver contributes to retinoic acid biosynthesis from β-apocarotenoic acids. J. Biol. Chem. 271, 26490-26498.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26490-26498
    • Wang, X.-D.1    Russell, R.M.2    Liu, C.3    Stickel, F.4    Smith, D.E.5    Krinsky, N.L.6
  • 12
    • 0028217849 scopus 로고
    • Retinoids and vertebrate development (Minireview)
    • 12. Gudas, L.J. (1994) Retinoids and vertebrate development (Minireview). J. Biol. Chem. 269, 15399-15402.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15399-15402
    • Gudas, L.J.1
  • 13
    • 0028841477 scopus 로고
    • Biotransformation of all-trans-retinol and all-trans-retinal to all-trans-retinoic acid in rat conceptal homogenates
    • 13. Chen, H., Namkung, M.J. & Juchau, M.R. (1995) Biotransformation of all-trans-retinol and all-trans-retinal to all-trans-retinoic acid in rat conceptal homogenates. Biochem. Pharmacol. 50, 1257-1264.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1257-1264
    • Chen, H.1    Namkung, M.J.2    Juchau, M.R.3
  • 14
    • 0026033598 scopus 로고
    • The metabolism of 3,7-dimethyl-2,6-octadiene (citral) in rat hepatic and cytosolic fractions. Interaction with aldehyde and alcohol dehydrogenases
    • 14. Boyer, C.S. & Petersen, D.R. (1991) The metabolism of 3,7-dimethyl-2,6-octadiene (citral) in rat hepatic and cytosolic fractions. Interaction with aldehyde and alcohol dehydrogenases. Drug Metab. Disposit. 19, 81-86.
    • (1991) Drug Metab. Disposit. , vol.19 , pp. 81-86
    • Boyer, C.S.1    Petersen, D.R.2
  • 15
    • 0023604469 scopus 로고
    • Human aldehyde dehydrogenase: Metabolism of putrescine and histamine
    • 15. Ambroziak, W. & Pietruszko, R. (1987) Human aldehyde dehydrogenase: metabolism of putrescine and histamine. Alcohol. Clin. Exp. Res. 11, 528-532.
    • (1987) Alcohol. Clin. Exp. Res. , vol.11 , pp. 528-532
    • Ambroziak, W.1    Pietruszko, R.2
  • 16
    • 0019945001 scopus 로고
    • Human aldehyde dehydrogenase: Improved purification procedure and comparison of homogeneous isozymes E1 and E2
    • 16. Hempel, J., Reed, D. & Pietruszko, R. (1982) Human aldehyde dehydrogenase: improved purification procedure and comparison of homogeneous isozymes E1 and E2. Alcohol. Clin. Expl. Res. 6, 417-425.
    • (1982) Alcohol. Clin. Expl. Res. , vol.6 , pp. 417-425
    • Hempel, J.1    Reed, D.2    Pietruszko, R.3
  • 17
    • 77049162117 scopus 로고
    • A microbiuret method for protein determination. Determination of total protein in cerebrospinal fluid
    • 17. Goa, J. (1953) A microbiuret method for protein determination. Determination of total protein in cerebrospinal fluid. Scand. J. Clin. Lab. Invest. 5, 218-222.
    • (1953) Scand. J. Clin. Lab. Invest. , vol.5 , pp. 218-222
    • Goa, J.1
  • 18
    • 0013561833 scopus 로고
    • A simple method for calculation of Km and V from a single reaction progress curve
    • 18. Yun, S.L. & Suelter, C.H. (1977) A simple method for calculation of Km and V from a single reaction progress curve. Biochim. Biophys. Acta 480, 324-337.
    • (1977) Biochim. Biophys. Acta , vol.480 , pp. 324-337
    • Yun, S.L.1    Suelter, C.H.2
  • 19
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • 19. Lineweaver, H. & Burk, D. (1934) The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56, 658-667.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-667
    • Lineweaver, H.1    Burk, D.2
  • 20
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • 20. Cleland, W.W. (1979) Statistical analysis of enzyme kinetic data. Meth. Enzymol. 63, 103-138.
    • (1979) Meth. Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 21
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • 22. Kitz, R. & Wilson, I.B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 237, 3245-3249.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 22
    • 84995023977 scopus 로고
    • The effect of enzyme concentration on the Michaelis-Menten equation
    • 23. Chaplin, M.F. (1981) The effect of enzyme concentration on the Michaelis-Menten equation. Trends Biochem. Sci. 6, R6.
    • (1981) Trends Biochem. Sci. , vol.6
    • Chaplin, M.F.1
  • 23
    • 0021249256 scopus 로고
    • Inhibition of human aldehyde dehydrogenase isozymes by propiolaldehyde
    • 25. Ferencz-Biro, K. & Pietruszko, R. (1984) Inhibition of human aldehyde dehydrogenase isozymes by propiolaldehyde. Alcohol. Clin. Expl. Res. 8, 302-307.
    • (1984) Alcohol. Clin. Expl. Res. , vol.8 , pp. 302-307
    • Ferencz-Biro, K.1    Pietruszko, R.2
  • 24
    • 0023090971 scopus 로고
    • Oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases
    • 21. Mitchell, D.Y. & Petersen, D.R. (1987) Oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol. Appl. Pharmacol. 87, 403-410.
    • (1987) Toxicol. Appl. Pharmacol. , vol.87 , pp. 403-410
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 26
    • 0026640782 scopus 로고
    • Biosynthesis of all-trans-retinoic acid from retinal
    • 26. Posch, K.C., Burns, R.D. & Napoli, J.L. (1992) Biosynthesis of all-trans-retinoic acid from retinal. J. Biol. Chem. 267, 19676-19682.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19676-19682
    • Posch, K.C.1    Burns, R.D.2    Napoli, J.L.3
  • 27
    • 0014517882 scopus 로고
    • Comparison of esterase activities of trypsin, plasmin and thrombin on guanidinobenzoate esters
    • 27. Chase, T. Jr & Shaw, E. (1969) Comparison of esterase activities of trypsin, plasmin and thrombin on guanidinobenzoate esters. Biochem. USA 8, 2212-2224.
    • (1969) Biochem. USA , vol.8 , pp. 2212-2224
    • Chase T., Jr.1    Shaw, E.2
  • 28
    • 0026539553 scopus 로고
    • Aldehyde dehydrogenase: Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis
    • 28. Blatter, E.E., Abriola, D.P. & Pietruszko, R. (1992) Aldehyde dehydrogenase: covalent intermediate in aldehyde dehydrogenation and ester hydrolysis. Biochem. J. 282, 353-360.
    • (1992) Biochem. J. , vol.282 , pp. 353-360
    • Blatter, E.E.1    Abriola, D.P.2    Pietruszko, R.3
  • 30
    • 0014986335 scopus 로고
    • Substrate characteristics of human liver aldehyde dehydrogenase
    • 30. Bodley, F.H. & Blair, A.H. (1971) Substrate characteristics of human liver aldehyde dehydrogenase. Can. J. Biochem. 49, 1-5.
    • (1971) Can. J. Biochem. , vol.49 , pp. 1-5
    • Bodley, F.H.1    Blair, A.H.2
  • 31
    • 0028037627 scopus 로고
    • Enzymic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases
    • 31. Chen, M., Achkar, C. & Gudas, L.J. (1994) Enzymic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases. Molec. Pharmacol. 46, 88-96.
    • (1994) Molec. Pharmacol. , vol.46 , pp. 88-96
    • Chen, M.1    Achkar, C.2    Gudas, L.J.3
  • 32
    • 0029863799 scopus 로고    scopus 로고
    • Kinetics and specificity of human liver aldehyde dehydrogenase towards aliphatic, arimatic and fused polycyclic aldehydes
    • 32. Klyosoff, A.A. (1996) Kinetics and specificity of human liver aldehyde dehydrogenase towards aliphatic, arimatic and fused polycyclic aldehydes. Biochem. USA 35, 4457-4467.
    • (1996) Biochem. USA , vol.35 , pp. 4457-4467
    • Klyosoff, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.