메뉴 건너뛰기




Volumn 143-144, Issue , 2003, Pages 85-91

Chemical modifications to study mutations that affect the ability of the general base (E268) to function in human liver mitochondrial aldehyde dehydrogenase

Author keywords

Aldehyde dehydrogenase; Asian variant of ALDH; Chemical modifications; Disulfiram analogs; General base

Indexed keywords

ALDEHYDE; ALDEHYDE DEHYDROGENASE; CYSTEINE; DISULFIRAM; NICOTINAMIDE ADENINE DINUCLEOTIDE; S METHYL N,N DIETHYLTHIOCARBAMOYLSULFOXIDE; SULFOXIDE; UNCLASSIFIED DRUG; WATER;

EID: 0345073750     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00177-1     Document Type: Conference Paper
Times cited : (6)

References (11)
  • 1
    • 0015499994 scopus 로고
    • Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity
    • Feldman R.I., Weiner H. Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity. J. Biol. Chem. 247:1972;267.
    • (1972) J. Biol. Chem. , vol.247 , pp. 267
    • Feldman, R.I.1    Weiner, H.2
  • 2
    • 0020488533 scopus 로고
    • Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1)
    • Hempel J., Pietruszko R., Fietzek P., Jörnvall H. Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1). Biochemistry. 21:1982;6834-6838.
    • (1982) Biochemistry , vol.21 , pp. 6834-6838
    • Hempel, J.1    Pietruszko, R.2    Fietzek, P.3    Jörnvall, H.4
  • 3
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residues of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • Farrés J., Wang T.T.Y., Cunningham S.J., Weiner H. Investigation of the active site cysteine residues of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry. 34:1995;2592-2598.
    • (1995) Biochemistry , vol.34 , pp. 2592-2598
    • Farrés, J.1    Wang, T.T.Y.2    Cunningham, S.J.3    Weiner, H.4
  • 4
    • 0025138339 scopus 로고
    • Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase
    • Abriola D.P., MacKerell A.D.J.R., Pietruszko R. Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase. Biochem. J. 266:1990;179-187.
    • (1990) Biochem. J. , vol.266 , pp. 179-187
    • Abriola, D.P.1    MacKerell, A.D.J.R.2    Pietruszko, R.3
  • 5
    • 0028922730 scopus 로고
    • Investigation of the role of glutamate 268 in human liver aldehyde dehydrogenase
    • Wang X.-P., Weiner H. Investigation of the role of glutamate 268 in human liver aldehyde dehydrogenase. Biochemistry. 34:1995;237-243.
    • (1995) Biochemistry , vol.34 , pp. 237-243
    • Wang, X.-P.1    Weiner, H.2
  • 6
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol adversion
    • Steinmetz C.G., Xie P., Weiner H., Hurley T.D. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol adversion. Structures. 5:1997;701-711.
    • (1997) Structures , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 7
    • 0017079051 scopus 로고
    • Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase
    • Weiner H., Hu J.H.J., Sanny C.G. Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase. J. Biol. Chem. 251:1976;3853.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3853
    • Weiner, H.1    Hu, J.H.J.2    Sanny, C.G.3
  • 8
    • 0034039653 scopus 로고    scopus 로고
    • Identification of the protein-drug adduct formed between aldehyde dehydrogenase and S-methyl-N,N-diethylthiocarbamoyl sulfoxide by on-line proteolytic digestion high performance liquid chromatography electrospray ionization mass spectrometry
    • Shen M.L., Johnson K.L., Mays D.C., Lipsky J.J., Naylor S. Identification of the protein-drug adduct formed between aldehyde dehydrogenase and S-methyl-N,N-diethylthiocarbamoyl sulfoxide by on-line proteolytic digestion high performance liquid chromatography electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 14:2000;918-923.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 918-923
    • Shen, M.L.1    Johnson, K.L.2    Mays, D.C.3    Lipsky, J.J.4    Naylor, S.5
  • 9
    • 0034624970 scopus 로고    scopus 로고
    • Cooperativity in NAD binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase
    • Wei B., Ni L., Hurley T.D., Weiner H. Cooperativity in NAD binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase. Biochemistry. 39:2000;5295-5302.
    • (2000) Biochemistry , vol.39 , pp. 5295-5302
    • Wei, B.1    Ni, L.2    Hurley, T.D.3    Weiner, H.4
  • 10
    • 0019878597 scopus 로고
    • NAD-activation of the esterase reaction of horse liver aldehyde dehydrogenase
    • Takahashi K., Weiner H. NAD-activation of the esterase reaction of horse liver aldehyde dehydrogenase. Biochemistry. 20:1981;2720-2726.
    • (1981) Biochemistry , vol.20 , pp. 2720-2726
    • Takahashi, K.1    Weiner, H.2
  • 11
    • 0030754023 scopus 로고    scopus 로고
    • Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase
    • Ni L., Sheikh S., Weiner H. Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272:1997;18823-18826.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18823-18826
    • Ni, L.1    Sheikh, S.2    Weiner, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.