메뉴 건너뛰기




Volumn 22, Issue 2, 2009, Pages 47-55

Purification and characterization of erythritol dehydrogenase from mycobacterium smegmatis

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; BACTERIAL ENZYME; BUFFER; CHELATING AGENT; CITRIC ACID; CYSTEINE; EDETIC ACID; ERYTHRITOL; ERYTHRITOL DEHYDROGENASE; GLYCINE; METALLOPROTEIN; OXIDOREDUCTASE; POLYOL; PYRIDINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; RIBITOL; TROMETAMOL; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 77953384392     PISSN: 08670609     EISSN: None     Source Type: Journal    
DOI: 10.2478/v10080-008-0177-8     Document Type: Article
Times cited : (4)

References (16)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem., 72, 248, 1976.
    • (1976) Anal. Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 2
    • 78651153791 scopus 로고    scopus 로고
    • Davis B.: Disc electrophoresis. II Method and application to human serum proteins. Ann N. Y. Acad. Sci., 121, 404, 1964.
    • Davis B.: Disc electrophoresis. II Method and application to human serum proteins. Ann N. Y. Acad. Sci., 121, 404, 1964.
  • 3
    • 34547763029 scopus 로고
    • The intermediary metabolism of the mycobacteria
    • Edson N. L.: The intermediary metabolism of the mycobacteria. Bacteriol. Rev., 15, 147, 1951.
    • (1951) Bacteriol. Rev , vol.15 , pp. 147
    • Edson, N.L.1
  • 5
    • 3242692281 scopus 로고    scopus 로고
    • Jakoby W. B., Fredericks J.: Erythritol dehydrogenase from Aerobacter aerogenes. BBA, 48, 26, 1961.
    • Jakoby W. B., Fredericks J.: Erythritol dehydrogenase from Aerobacter aerogenes. BBA, 48, 26, 1961.
  • 6
    • 0038493652 scopus 로고    scopus 로고
    • Purification and characterization of a novel erythrose reductase from Candida magnoliae
    • Jung - Kul L. et al.: Purification and characterization of a novel erythrose reductase from Candida magnoliae. Appl. Environ. Microbiol., 69 (7), 3710, 2003.
    • (2003) Appl. Environ. Microbiol , vol.69 , Issue.7 , pp. 3710
    • Jung - Kul, L.1
  • 7
    • 0037295126 scopus 로고    scopus 로고
    • Functional expression and characterization of EryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate
    • Lillo A. M. et al.: Functional expression and characterization of EryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate. Bioorg. Med. Chem. Lett., 13, 737, 2003.
    • (2003) Bioorg. Med. Chem. Lett , vol.13 , pp. 737
    • Lillo, A.M.1
  • 8
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O. et al.: Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265, 1956.
    • (1956) J. Biol. Chem , vol.193 , pp. 265
    • Lowry, O.1
  • 9
    • 0036481377 scopus 로고    scopus 로고
    • L-erythrulose production by oxidative fermentation is catalyzed by PQQ-containing membrane-bound dehydrogenase
    • Moonmangmee D. et al.: L-erythrulose production by oxidative fermentation is catalyzed by PQQ-containing membrane-bound dehydrogenase. Biosci. Biotechnol. Biochem., 66 (2), 307, 2002.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , Issue.2 , pp. 307
    • Moonmangmee, D.1
  • 10
    • 0032411028 scopus 로고    scopus 로고
    • Erythritol: An interpretive summary of biochemical, metabolic, toxicological and clinical data
    • Munro I. C. et al.: Erythritol: An interpretive summary of biochemical, metabolic, toxicological and clinical data. Food and Chemical Toxicology, 36, 1139, 1998.
    • (1998) Food and Chemical Toxicology , vol.36 , pp. 1139
    • Munro, I.C.1
  • 11
    • 33745787551 scopus 로고    scopus 로고
    • Identification of enzyme responsible for erythritol utilization and reaction product in yeast Lipomyces starkeyi
    • Nishimura K. et al.: Identification of enzyme responsible for erythritol utilization and reaction product in yeast Lipomyces starkeyi. J. Biosci. Bioeng., 101 (4), 303, 2006.
    • (2006) J. Biosci. Bioeng , vol.101 , Issue.4 , pp. 303
    • Nishimura, K.1
  • 12
    • 77953386888 scopus 로고    scopus 로고
    • Initial studies on a novel pathway for erythritol catabolism in
    • Annales UMCS, sect. DDD
    • Paradowska K. et al.: Initial studies on a novel pathway for erythritol catabolism in Mycobacterium smegmatis. Annales UMCS, sect. DDD, 14, 93, 2001.
    • (2001) Mycobacterium smegmatis , vol.14 , pp. 93
    • Paradowska, K.1
  • 13
    • 77953379815 scopus 로고    scopus 로고
    • Paradowska K., Swatko M.: Induction and substrate specificity of erythritol dehydrogenase from Mycobacterium smegmatis ATCC 20. Annales UMCS, sect. DDD, 15, 107, 2002.
    • Paradowska K., Swatko M.: Induction and substrate specificity of erythritol dehydrogenase from Mycobacterium smegmatis ATCC 20. Annales UMCS, sect. DDD, 15, 107, 2002.
  • 15
    • 77953432313 scopus 로고    scopus 로고
    • Isolation and partial characterization of a novel ribitol dehydrogenase from mycobacteria. Annales UMCS, sect. DDD
    • Swatko M., Szumiło T.: Isolation and partial characterization of a novel ribitol dehydrogenase from mycobacteria. Annales UMCS, sect. DDD, 12/13, 169, 1999/2000.
    • (1999) , vol.12-13 , pp. 169
    • Swatko, M.1    Szumiło, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.