메뉴 건너뛰기




Volumn 28, Issue 1, 1997, Pages 29-40

NADP-dependent enzymes. II: Evolution of the mono- and dinucleotide binding domains

Author keywords

dinucleotide bonding domains; molecular evolution; mononucleotide binding domains; nicotinamide adenine dinucleotide; nicotinamide adenine dinucleotide phosphate

Indexed keywords

3ALPHA(OR 20BETA) HYDROXYSTEROID DEHYDROGENASE; ALCOHOL DEHYDROGENASE; ALDEHYDE REDUCTASE; CATALASE; DIHYDROFOLATE REDUCTASE; DIHYDROPTERIDINE REDUCTASE; FORMATE DEHYDROGENASE; GLUTATHIONE REDUCTASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PEROXIDASE; PHOSPHOGLUCONATE DEHYDROGENASE; TRICHOSANTHIN;

EID: 0030972646     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199705)28:1<29::AID-PROT3>3.0.CO;2-E     Document Type: Article
Times cited : (55)

References (21)
  • 2
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol, W.G.J., van Duijnen, P.T., Berendsen, H.J.C. The α-helix dipole and the properties of proteins. Nature 273: 443-446, 1978.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 3
    • 0019053306 scopus 로고
    • Relation between structure and function of α/β proteins
    • Branden, C.I. Relation between structure and function of α/β proteins. Q. Rev. Biophys. 13:317-338, 1980.
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 317-338
    • Branden, C.I.1
  • 5
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A.M. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5:775-783, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 6
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann, M.G., Moras, D., Olsen, K. Chemical and biological evolution of a nucleotide-binding protein. Nature 250:194-199, 1974.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.3
  • 7
    • 0016283234 scopus 로고
    • Structural and functional similarities within the coenzyme binding domains of dehydrogenases
    • Ohlsson, I., Nordstrom, B., Branden, C.I. Structural and functional similarities within the coenzyme binding domains of dehydrogenases. J. Mol. Biol. 89:339-354, 1974.
    • (1974) J. Mol. Biol. , vol.89 , pp. 339-354
    • Ohlsson, I.1    Nordstrom, B.2    Branden, C.I.3
  • 8
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: Prototype for a structurally novel flavoenzyme family. Science 251:60-66, 1991.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.H.2    Herriot, J.R.3
  • 10
    • 0029198395 scopus 로고
    • Eukaryotic dihydrofolate reductase
    • Blakley, R.L. Eukaryotic dihydrofolate reductase. Adv. Enzymol. 70:23-102, 1995.
    • (1995) Adv. Enzymol. , vol.70 , pp. 23-102
    • Blakley, R.L.1
  • 11
    • 0018805382 scopus 로고
    • Structural comparisons of heme binding proteins
    • Argos, P., Rossmann, M.G. Structural comparisons of heme binding proteins. Biochemistry 18:4951-4960, 1979.
    • (1979) Biochemistry , vol.18 , pp. 4951-4960
    • Argos, P.1    Rossmann, M.G.2
  • 12
    • 0017187837 scopus 로고
    • Exploring structural homology of proteins
    • Rossmann, M.G., Argos, P. Exploring structural homology of proteins. J. Mol. Biol. 105:75-95, 1976.
    • (1976) J. Mol. Biol. , vol.105 , pp. 75-95
    • Rossmann, M.G.1    Argos, P.2
  • 13
    • 0000615015 scopus 로고
    • Use of the estimated errors of the data in structure-correlation studies
    • Carugo, O. Use of the estimated errors of the data in structure-correlation studies. Acta Crystallogr. B51:314-328, 1995.
    • (1995) Acta Crystallogr. , vol.B51 , pp. 314-328
    • Carugo, O.1
  • 16
    • 0015457677 scopus 로고
    • The aromatic binding site in subtilisin BNP' and its resemblance to chymotrypsin
    • Cold Spring Harbor, NY: The Cold Spring Harbor Laboratory
    • Kraut, J., Robertus, J.D., Birktoft, J.J., Alden, R.A., Wilcox, P.E., Powers, J.C. The aromatic binding site in subtilisin BNP' and its resemblance to chymotrypsin. In "Cold Spring Harbor Symposia on Quantitative Biology." Vol. XXXVI. Cold Spring Harbor, NY: The Cold Spring Harbor Laboratory, 1972:117-423.
    • (1972) Cold Spring Harbor Symposia on Quantitative Biology , vol.36 , pp. 117-423
    • Kraut, J.1    Robertus, J.D.2    Birktoft, J.J.3    Alden, R.A.4    Wilcox, P.E.5    Powers, J.C.6
  • 17
    • 0018072848 scopus 로고
    • The taxonomy of binding sites in proteins
    • Rossmann, M.G., Argos, P. The taxonomy of binding sites in proteins. Mol. Cell. Biochem. 21:161-182, 1978.
    • (1978) Mol. Cell. Biochem. , vol.21 , pp. 161-182
    • Rossmann, M.G.1    Argos, P.2
  • 18
    • 0027457706 scopus 로고
    • SRS, an indexing and retrieval tool for flat file data libraries
    • Etzold, T., Argos, P. SRS, an indexing and retrieval tool for flat file data libraries. Comput. Appl. Biosci. 9:49-57, 1993.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 49-57
    • Etzold, T.1    Argos, P.2
  • 19
    • 0027523415 scopus 로고
    • Transforming a set of biological flat file libraries to a fast access network
    • Etzold, T., Argos, P. Transforming a set of biological flat file libraries to a fast access network. Comput. Appl. Biosci. 9:59-64, 1993.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 59-64
    • Etzold, T.1    Argos, P.2
  • 20
    • 0029619259 scopus 로고
    • Knowledge-based secondary structure assignment
    • Frishman, D., Argos, P. Knowledge-based secondary structure assignment. Proteins 23:566-579, 1995.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.