메뉴 건너뛰기




Volumn 271, Issue 1, 2007, Pages 78-82

Mutational analysis of NADH-binding residues in triphenylmethane reductase from Citrobacter sp. strain KCTC 18061P

Author keywords

Cofactor; Site directed mutagenesis; Triphenylmethane reductase

Indexed keywords

ALANINE; GLYCINE; MUTANT PROTEIN; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRIPHENYLMETHANE REDUCTASE; UNCLASSIFIED DRUG;

EID: 34247882914     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.00709.x     Document Type: Article
Times cited : (5)

References (26)
  • 1
    • 0018397045 scopus 로고
    • Further study of the genetic toxicology of gentian violet
    • Au W, Butler MA, Bloom SF Matmey TS (1979) Further study of the genetic toxicology of gentian violet. Mutat Res 66 : 103 112.
    • (1979) Mutat Res , vol.66 , pp. 103-112
    • Au, W.1    Butler, M.A.2    Bloom, S.F.3    Matmey, T.S.4
  • 3
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution
    • Bauer AJ, Rayment I, Frey PA Holden HM (1992) The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution. Proteins 12 : 372 381.
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 4
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins
    • Bellamacina CR (1996) The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J 10 : 1257 1269.
    • (1996) FASEB J , vol.10 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 5
    • 0024413884 scopus 로고
    • Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution
    • Birktoft JJ, Rhodes G Banaszak LJ (1989) Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution. Biochemistry 28 : 6065 6081.
    • (1989) Biochemistry , vol.28 , pp. 6065-6081
    • Birktoft, J.J.1    Rhodes, G.2    Banaszak, L.J.3
  • 6
    • 0043164772 scopus 로고    scopus 로고
    • Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24
    • Blümel S Stolz A (2003) Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl Microbiol Biotechnol 62 : 186 190.
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 186-190
    • Blümel, S.1    Stolz, A.2
  • 7
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • Blümel S, Knackmuss HJ Stolz A (2002) Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl Environ Microbiol 68 : 3948 3955.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3948-3955
    • Blümel, S.1    Knackmuss, H.J.2    Stolz, A.3
  • 8
    • 0024004825 scopus 로고
    • Biodegradation of crystal violet by the white rot fungus Phanerochaete chrysosporium
    • Bumpus JA Brock BJ (1988) Biodegradation of crystal violet by the white rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol 54 : 1143 1150.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1143-1150
    • Bumpus, J.A.1    Brock, B.J.2
  • 9
    • 0025829758 scopus 로고
    • Enhancing effect of malachite green on the development of hepatic pre-neoplastic lesions induced by N-nitrosodiethylamine in rats
    • Fernandes C, Lalitha VS Rao KVK (1991) Enhancing effect of malachite green on the development of hepatic pre-neoplastic lesions induced by N-nitrosodiethylamine in rats. Carcinogenesis 12 : 839 845.
    • (1991) Carcinogenesis , vol.12 , pp. 839-845
    • Fernandes, C.1    Lalitha, V.S.2    Rao, K.V.K.3
  • 10
    • 0033548685 scopus 로고    scopus 로고
    • Evolution of plant defense mechanisms: Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases
    • Gang DR, Kasahara H, Xia ZQ, Vander Mijnsbrugge K, Bauw G, Boerjan W, Van Montagu M, Davin LB Lewis NG (1999) Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases. J Biol Chem 27 : 7516 7527.
    • (1999) J Biol Chem , vol.27 , pp. 7516-7527
    • Gang, D.R.1    Kasahara, H.2    Xia, Z.Q.3    Vander Mijnsbrugge, K.4    Bauw, G.5    Boerjan, W.6    Van Montagu, M.7    Davin, L.B.8    Lewis, N.G.9
  • 11
    • 0001033436 scopus 로고
    • Dyes and dye intermediates
    • Kroschwitz, J.I., ed), pp. John Wiley & Sons, New York.
    • Gregory P (1993) Dyes and dye intermediates. Encyclopedia of Chemical Technology (Kroschwitz JI, ed), pp. 544 545. John Wiley & Sons, New York.
    • (1993) Encyclopedia of Chemical Technology , pp. 544-545
    • Gregory, P.1
  • 12
    • 29144452195 scopus 로고    scopus 로고
    • Triphenylmethane reductase from Citrobacter sp. strain KCTC 18061P: Purification, characterization, gene cloning, and overexpression of a functional protein in Escherichia coli
    • Jang MS, Lee YM, Kim CH, Lee JH, Kang DW, Kim SJ Lee YC (2005) Triphenylmethane reductase from Citrobacter sp. strain KCTC 18061P: purification, characterization, gene cloning, and overexpression of a functional protein in Escherichia coli. Appl Environ Microbiol 71 : 7955 7960.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7955-7960
    • Jang, M.S.1    Lee, Y.M.2    Kim, C.H.3    Lee, J.H.4    Kang, D.W.5    Kim, S.J.6    Lee, Y.C.7
  • 13
    • 0025996527 scopus 로고
    • Structure of the Hordeum vulgare gene encoding dihydroflavonol-4- reductase and molecular analysis of ant18 mutants blocked in flavonoid synthesis
    • Kristiansen KN Rohde W (1991) Structure of the Hordeum vulgare gene encoding dihydroflavonol-4-reductase and molecular analysis of ant18 mutants blocked in flavonoid synthesis. Mol Gen Genet 230 : 49 59.
    • (1991) Mol Gen Genet , vol.230 , pp. 49-59
    • Kristiansen, K.N.1    Rohde, W.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0026245210 scopus 로고
    • Stress responses in alfalfa (Medicago sativa L.) 11. Molecular cloning and expression of alfalfa isoflavone reductase, a key enzyme of isoflavonoid phytoalexin biosynthesis
    • Paiva NL, Edwards R, Sun YJ, Hrazdina G Dixon RA (1991) Stress responses in alfalfa (Medicago sativa L.) 11. Molecular cloning and expression of alfalfa isoflavone reductase, a key enzyme of isoflavonoid phytoalexin biosynthesis. Plant Mol Biol 17 : 653 667.
    • (1991) Plant Mol Biol , vol.17 , pp. 653-667
    • Paiva, N.L.1    Edwards, R.2    Sun, Y.J.3    Hrazdina, G.4    Dixon, R.A.5
  • 18
    • 0027991002 scopus 로고
    • Flavin reductase: Sequence of cDNA from bovine liver and tissue distribution
    • Quandt KS Hultquist DE (1994) Flavin reductase: sequence of cDNA from bovine liver and tissue distribution. Proc Natl Acad Sci USA 91 : 9322 9326.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9322-9326
    • Quandt, K.S.1    Hultquist, D.E.2
  • 19
    • 0029619154 scopus 로고
    • Inhibition of DNA synthesis in primary rat hepatocyte cultures by malachite green: A new liver tumor promoter
    • Rao KVK (1995) Inhibition of DNA synthesis in primary rat hepatocyte cultures by malachite green: a new liver tumor promoter. Toxicol Lett 81 : 107 113.
    • (1995) Toxicol Lett , vol.81 , pp. 107-113
    • Rao, K.V.K.1
  • 20
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D Olsen KW (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250 : 194 199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 21
    • 0028937651 scopus 로고
    • Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase
    • Scapin G, Blanchard JS Sacchettini JC (1995) Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34 : 3502 3512.
    • (1995) Biochemistry , vol.34 , pp. 3502-3512
    • Scapin, G.1    Blanchard, J.S.2    Sacchettini, J.C.3
  • 22
    • 1642264258 scopus 로고    scopus 로고
    • Isolation and characterization of microorganisms capable of decolorizing various triphenylmethane dyes
    • Sharma DK, Saini HS, Singh M, Chimni SS Chadha BS (2004) Isolation and characterization of microorganisms capable of decolorizing various triphenylmethane dyes. J Basic Microbiol 44 : 59 65.
    • (2004) J Basic Microbiol , vol.44 , pp. 59-65
    • Sharma, D.K.1    Saini, H.S.2    Singh, M.3    Chimni, S.S.4    Chadha, B.S.5
  • 23
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N, Nonaka T, Nakanishi M, Deyashiki Y, Hara A Mitsui Y (1996) Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4 : 33 45.
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 24
    • 0028947149 scopus 로고
    • Decolorization of triphenylmethane dyes by the birds nest fungus Cyathus bulleri
    • Vasdev K, Kuhad RC Saxena RK (1995) Decolorization of triphenylmethane dyes by the birds nest fungus Cyathus bulleri. Curr Microbiol 30 : 269 272.
    • (1995) Curr Microbiol , vol.30 , pp. 269-272
    • Vasdev, K.1    Kuhad, R.C.2    Saxena, R.K.3
  • 25
    • 33646078348 scopus 로고    scopus 로고
    • Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.)
    • Wang X, He X, Lin J, Shao H, Chang Z Dixon RA (2006) Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.). J Mol Biol 358 : 1341 1352.
    • (2006) J Mol Biol , vol.358 , pp. 1341-1352
    • Wang, X.1    He, X.2    Lin, J.3    Shao, H.4    Chang, Z.5    Dixon, R.A.6
  • 26
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga RK, Terpstra P Hol WGJ (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 187 : 101 107.
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.