메뉴 건너뛰기




Volumn 62, Issue 7, 1996, Pages 2405-2410

Analysis of interaction between the Arthrobacter sarcosine oxidase and the coenzyme flavin adenine dinucleotide by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; FLAVINE ADENINE NUCLEOTIDE; OXIDOREDUCTASE; SARCOSINE;

EID: 0029957052     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.7.2405-2410.1996     Document Type: Article
Times cited : (26)

References (32)
  • 1
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y., and G. D. Fasman. 1978. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47:45-148.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 2
    • 0021215077 scopus 로고
    • Effect of monovalent anions on the mechanism of phenol hydroxylase
    • Detmer, K., and V. Massey. 1984. Effect of monovalent anions on the mechanism of phenol hydroxylase. J. Biol. Chem. 259:11265-11272.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11265-11272
    • Detmer, K.1    Massey, V.2
  • 3
    • 0025363898 scopus 로고
    • Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria
    • Dietrichs, M., M. Meyer, B. Schmidt, and J. R. Andreesen. 1990. Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria. J. Bacteriol. 172:2088-2095.
    • (1990) J. Bacteriol. , vol.172 , pp. 2088-2095
    • Dietrichs, M.1    Meyer, M.2    Schmidt, B.3    Andreesen, J.R.4
  • 4
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla, S., and V. Massey. 1989. Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181:1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 5
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., H. Nojima, and H. Okayama. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 7
    • 0023644992 scopus 로고
    • Refined structure of glutathione reductase at 1.54 Å resolution
    • Karplus, P. A., and G. E. Schulz. 1987. Refined structure of glutathione reductase at 1.54 Å resolution. J. Mol. Biol. 195:701-729.
    • (1987) J. Mol. Biol. , vol.195 , pp. 701-729
    • Karplus, P.A.1    Schulz, G.E.2
  • 8
    • 0011435093 scopus 로고
    • Crystallization and characterization of sarcosine oxidase from Alcaligenes denitrificans subsp. denitrificans
    • Kim, J. M., S. Shimizu, and H. Yamada. 1987. Crystallization and characterization of sarcosine oxidase from Alcaligenes denitrificans subsp. denitrificans. Agric. Biol. Chem. 51:1167-1168.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 1167-1168
    • Kim, J.M.1    Shimizu, S.2    Yamada, H.3
  • 9
    • 0019123154 scopus 로고
    • A fluorophotometric determination of serum creatinine and creatine using a creatinineamidohydrolase-creatineamidinohydrolase-sarcosine oxidase-peroxidase system and diacetyldichlorofluorescin
    • Kinoshita, T., and Y. Hiraga. 1980. A fluorophotometric determination of serum creatinine and creatine using a creatinineamidohydrolase-creatineamidinohydrolase-sarcosine oxidase-peroxidase system and diacetyldichlorofluorescin. Chem. Pharm. Bull. 28:3501-3506.
    • (1980) Chem. Pharm. Bull. , vol.28 , pp. 3501-3506
    • Kinoshita, T.1    Hiraga, Y.2
  • 12
    • 0025816177 scopus 로고
    • Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution
    • Mattevi, A., A. J. Schierbeek, and W. G. J. Hol. 1991. Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution. J. Mol. Biol. 220:975-994.
    • (1991) J. Mol. Biol. , vol.220 , pp. 975-994
    • Mattevi, A.1    Schierbeek, A.J.2    Hol, W.G.J.3
  • 13
    • 84920301971 scopus 로고
    • Purification and propertics of sarcosine oxidase from Cylindrocarpon didymum M-1
    • Mori, N., M. Sano, Y. Tani, and H. Yamada. 1980. Purification and propertics of sarcosine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44:1391-1397.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1391-1397
    • Mori, N.1    Sano, M.2    Tani, Y.3    Yamada, H.4
  • 14
    • 0020712865 scopus 로고
    • Effect of anions, chaotropes, and phenol on the attachment of flavin adenine dinucleotide to phenol hydroxylase
    • Neujahr, H. Y. 1983. Effect of anions, chaotropes, and phenol on the attachment of flavin adenine dinucleotide to phenol hydroxylase. Biochemistry 22:580-584.
    • (1983) Biochemistry , vol.22 , pp. 580-584
    • Neujahr, H.Y.1
  • 15
    • 0025164672 scopus 로고
    • Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene
    • Nishiya, Y., and T. Imanaka. 1990. Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene. J. Bacteriol. 172:4861-4869.
    • (1990) J. Bacteriol. , vol.172 , pp. 4861-4869
    • Nishiya, Y.1    Imanaka, T.2
  • 16
    • 0027251385 scopus 로고
    • Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826
    • Nishiya, Y., and T. Imanaka. 1993. Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826. J. Ferment. Bioeng. 75:239-244.
    • (1993) J. Ferment. Bioeng. , vol.75 , pp. 239-244
    • Nishiya, Y.1    Imanaka, T.2
  • 17
    • 0028149977 scopus 로고
    • Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis
    • Nishiya, Y., and T. Imanaka. 1994. Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis. Appl. Environ. Microbiol. 60:4213-4215.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4213-4215
    • Nishiya, Y.1    Imanaka, T.2
  • 18
    • 0028796479 scopus 로고
    • Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues
    • Nishiya, Y., and T. Imanaka. 1995. Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues. Appl. Environ. Microbiol. 61:367-370.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 367-370
    • Nishiya, Y.1    Imanaka, T.2
  • 19
    • 0022885504 scopus 로고
    • Ion-selective membrane electrodes for clinical use
    • Oesch, U., D. Ammann, and W. Simon. 1986. Ion-selective membrane electrodes for clinical use. Clin. Chem. 32:1448-1459.
    • (1986) Clin. Chem. , vol.32 , pp. 1448-1459
    • Oesch, U.1    Ammann, D.2    Simon, W.3
  • 20
    • 0011394926 scopus 로고
    • Sarcosine oxidase from Arthrobacter ureafaciens: Purification and some properties
    • Ogushi, S., K. Nagao, S. Emi, M. Ando, and D. Tsuru. 1988. Sarcosine oxidase from Arthrobacter ureafaciens: purification and some properties. Chem. Pharm. Bull. 36:1445-1450.
    • (1988) Chem. Pharm. Bull. , vol.36 , pp. 1445-1450
    • Ogushi, S.1    Nagao, K.2    Emi, S.3    Ando, M.4    Tsuru, D.5
  • 22
    • 0018595232 scopus 로고
    • Creatinine amidohydrolase (creatininase) from Pseudomonas putida
    • Rikitake, K., I. Oka, M. Ando, T. Yoshimoto, and D. Tsuru. 1979. Creatinine amidohydrolase (creatininase) from Pseudomonas putida. J. Biochem. 86: 1109-1117.
    • (1979) J. Biochem. , vol.86 , pp. 1109-1117
    • Rikitake, K.1    Oka, I.2    Ando, M.3    Yoshimoto, T.4    Tsuru, D.5
  • 24
    • 0000091363 scopus 로고
    • A simple and accurate method for the determination of chloride in biological fluids
    • Schales, O., and A. A. Schales. 1941. A simple and accurate method for the determination of chloride in biological fluids. J. Biol. Chem. 140:879-884.
    • (1941) J. Biol. Chem. , vol.140 , pp. 879-884
    • Schales, O.1    Schales, A.A.2
  • 25
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution
    • Schreuder, H. A., P. A. Prick, R. K. Wierenda, G. Vriend, K. S. Wilson, W. G. J. Hol, and J. Drenth. 1989. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. J. Mol. Biol. 208:679-696.
    • (1989) J. Mol. Biol. , vol.208 , pp. 679-696
    • Schreuder, H.A.1    Prick, P.A.2    Wierenda, R.K.3    Vriend, G.4    Wilson, K.S.5    Hol, W.G.J.6    Drenth, J.7
  • 26
    • 0019454713 scopus 로고
    • Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96
    • Suzuki, M. 1981. Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. 89:599-607.
    • (1981) J. Biochem. , vol.89 , pp. 599-607
    • Suzuki, M.1
  • 27
    • 0023971592 scopus 로고
    • X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 Å resolution by molecular replacement method
    • Takenaka, A., K. Kizawa, T. Hata, S. Sato, E. Misaka, C. Tamuram, and Y. Sasada. 1988. X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 Å resolution by molecular replacement method. J. Biochem. 103:463-469.
    • (1988) J. Biochem. , vol.103 , pp. 463-469
    • Takenaka, A.1    Kizawa, K.2    Hata, T.3    Sato, S.4    Misaka, E.5    Tamuram, C.6    Sasada, Y.7
  • 30
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution
    • Vrielink, A., L. F. Lloyd, and D. M. Blow. 1991. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution. J. Mol. Biol. 219:533-554.
    • (1991) J. Mol. Biol. , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 31
    • 0023971911 scopus 로고
    • Lipoamide dehydrogenase from Azotobacter vinelandii: Molecular cloning, organisation and sequence analysis of the gene
    • Westphal, A. H., and A. De Kok. 1988. Lipoamide dehydrogenase from Azotobacter vinelandii: molecular cloning, organisation and sequence analysis of the gene. Eur. J. Biochem. 172:299-305.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 299-305
    • Westphal, A.H.1    De Kok, A.2
  • 32
    • 0021095474 scopus 로고
    • Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD as well as NADPH-binding domains of glutathione reductase
    • Wierenga, R. K., J. Drenth, and G. E. Schulz. 1983. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD as well as NADPH-binding domains of glutathione reductase. J. Mol. Biol. 167:725-739.
    • (1983) J. Mol. Biol. , vol.167 , pp. 725-739
    • Wierenga, R.K.1    Drenth, J.2    Schulz, G.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.