메뉴 건너뛰기




Volumn 70, Issue 12, 2004, Pages 7561-7566

Effects of expression of hemA and hemB genes on production of porphyrin in Propionibacterium freudenreichii

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; DAIRY PRODUCTS; FERMENTATION; STRAIN; VECTORS;

EID: 10444266006     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.12.7561-7566.2004     Document Type: Article
Times cited : (26)

References (29)
  • 1
    • 0001157711 scopus 로고
    • 14C 5-aminolevulinic acid from labeled precursors in greening plant tissues
    • 14C 5-aminolevulinic acid from labeled precursors in greening plant tissues. Plant Physiol. 53:297-303.
    • (1974) Plant Physiol. , vol.53 , pp. 297-303
    • Beale, S.I.1    Castelfranco, P.A.2
  • 2
    • 0033214249 scopus 로고    scopus 로고
    • Characterization of the Rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli
    • Bolt, E. L., L. Kryszak, J. Zeilstra-Ryalls, P. M. Shoolingin-Jordan, and M. J. Warren. 1999. Characterization of the Rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli. Eur. J. Biochem. 265:290-299.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 290-299
    • Bolt, E.L.1    Kryszak, L.2    Zeilstra-Ryalls, J.3    Shoolingin-Jordan, P.M.4    Warren, M.J.5
  • 3
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0015542618 scopus 로고
    • Porphyrin-accumulating mutants of Escherichia coli
    • Cox, R., and H. P. Charles. 1973. Porphyrin-accumulating mutants of Escherichia coli. J. Bacteriol. 113:122-132.
    • (1973) J. Bacteriol. , vol.113 , pp. 122-132
    • Cox, R.1    Charles, H.P.2
  • 5
    • 0030989127 scopus 로고    scopus 로고
    • The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme
    • Hashimoto, Y., M. Yamashita, and Y. Murooka. 1997. The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme. Appl. Microbiol. Biotechnol. 47:385-392.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 385-392
    • Hashimoto, Y.1    Yamashita, M.2    Murooka, Y.3
  • 6
    • 0029796424 scopus 로고    scopus 로고
    • Characterization of the hemB gene encoding δ-aminolevulinic acid dehydratase from Propionibacterium freudenreichii
    • Hashimoto, Y., M. Yamashita, H. Ono, and Y. Murooka. 1996. Characterization of the hemB gene encoding δ-aminolevulinic acid dehydratase from Propionibacterium freudenreichii. J. Ferment. Bioeng. 82:93-100.
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 93-100
    • Hashimoto, Y.1    Yamashita, M.2    Ono, H.3    Murooka, Y.4
  • 7
    • 0026526699 scopus 로고
    • Enzymatic basis of thiol-stimulated secretion of porphyrins by Escherichia coli
    • Javor, G. T., and E. F. Febre. 1992. Enzymatic basis of thiol-stimulated secretion of porphyrins by Escherichia coli. J. Bacteriol. 174:1072-1075.
    • (1992) J. Bacteriol. , vol.174 , pp. 1072-1075
    • Javor, G.T.1    Febre, E.F.2
  • 8
    • 0033025509 scopus 로고    scopus 로고
    • Organization of genes for tetrapyrrole biosynthesis in Gram-positive bacteria
    • Johansson, P., and L. Hederstedt. 1999. Organization of genes for tetrapyrrole biosynthesis in Gram-positive bacteria. Microbiology 145:529-538.
    • (1999) Microbiology , vol.145 , pp. 529-538
    • Johansson, P.1    Hederstedt, L.2
  • 9
    • 0020362218 scopus 로고
    • Uroporphyrinogen III cosynthetase: A direct assay method
    • Jordan, P. M. 1982. Uroporphyrinogen III cosynthetase: a direct assay method. Enzyme 28:158-169.
    • (1982) Enzyme , vol.28 , pp. 158-169
    • Jordan, P.M.1
  • 10
    • 0024286698 scopus 로고
    • Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon
    • Jordan, P. M., B. I. Mgbeje, S. D. Thomas, and A. F. Alwan. 1988. Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon. Biochem. J. 249:613-616.
    • (1988) Biochem. J. , vol.249 , pp. 613-616
    • Jordan, P.M.1    Mgbeje, B.I.2    Thomas, S.D.3    Alwan, A.F.4
  • 11
    • 0018290726 scopus 로고
    • The biosynthesis of uroporphyrinogen III: Order of assembly of the four porphobilinogen molecules in the formation of the tetrapyrrole ring
    • Jordan, P. M., and J. S. Seehra. 1979. The biosynthesis of uroporphyrinogen III: order of assembly of the four porphobilinogen molecules in the formation of the tetrapyrrole ring. FEBS Lett. 104:364-366.
    • (1979) FEBS Lett. , vol.104 , pp. 364-366
    • Jordan, P.M.1    Seehra, J.S.2
  • 12
    • 0033765883 scopus 로고    scopus 로고
    • Characterization of pRGO1, a plasmid from Propionibacterium acidipropionici, and its use for development of a host-vector system in propionibacteria
    • Kiatpapan, P., Y. Hashimoto, H. Nakamura, Y.-Z. Piao, H. Ono, M. Yamashita, and Y. Murooka. 2000. Characterization of pRGO1, a plasmid from Propionibacterium acidipropionici, and its use for development of a host-vector system in propionibacteria. Appl. Environ. Microbiol. 66:4688-4695.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4688-4695
    • Kiatpapan, P.1    Hashimoto, Y.2    Nakamura, H.3    Piao, Y.-Z.4    Ono, H.5    Yamashita, M.6    Murooka, Y.7
  • 13
    • 0034911171 scopus 로고    scopus 로고
    • Construction of an expression vector for propionibacteria and its use in production of 5-aminolevulinic acid by Propionibacterium freudenreichii
    • Kiatpapan, P., and Y. Murooka. 2001. Construction of an expression vector for propionibacteria and its use in production of 5-aminolevulinic acid by Propionibacterium freudenreichii. Appl. Microbiol. Biotechnol. 56:144-149.
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 144-149
    • Kiatpapan, P.1    Murooka, Y.2
  • 14
    • 0035666518 scopus 로고    scopus 로고
    • Heterologous expression of a gene encoding cholesterol oxidase in probiotic strains of Lactobacillus plantarum and Propionibacterium freudenreichii under the control of native promoters
    • Kiatpapan, P., M. Yamashita, N. Kawaraichi, T. Yasuda, and Y. Murooka. 2001. Heterologous expression of a gene encoding cholesterol oxidase in probiotic strains of Lactobacillus plantarum and Propionibacterium freudenreichii under the control of native promoters. J. Biosci. Bioeng. 95:459-465.
    • (2001) J. Biosci. Bioeng. , vol.95 , pp. 459-465
    • Kiatpapan, P.1    Yamashita, M.2    Kawaraichi, N.3    Yasuda, T.4    Murooka, Y.5
  • 15
    • 0021165517 scopus 로고
    • Influence of pH on porphyrin production in Propionibacterium acnes
    • Kjeldstad, B., A. Johnsson, and S. Sandberg. 1984. Influence of pH on porphyrin production in Propionibacterium acnes. Arch. Dermatol. Res. 276:396-400.
    • (1984) Arch. Dermatol. Res. , vol.276 , pp. 396-400
    • Kjeldstad, B.1    Johnsson, A.2    Sandberg, S.3
  • 16
    • 0020420409 scopus 로고
    • Comparisons and modifications of the colorimetric assay for delta-aminolevulinic acid synthase
    • Lien, L. F., and D. S. Beattie. 1982. Comparisons and modifications of the colorimetric assay for delta-aminolevulinic acid synthase. Enzyme 28:120-132.
    • (1982) Enzyme , vol.28 , pp. 120-132
    • Lien, L.F.1    Beattie, D.S.2
  • 17
    • 0023805538 scopus 로고
    • High-performance liquid chromatography of porphyrins
    • Lim, C. K., F. M. Li, and T. J. Peters. 1988. High-performance liquid chromatography of porphyrins. J. Chromatogr. 429:123-153.
    • (1988) J. Chromatogr. , vol.429 , pp. 123-153
    • Lim, C.K.1    Li, F.M.2    Peters, T.J.3
  • 18
    • 78651057641 scopus 로고
    • The occurrence and determination of 5-aminolevulinic acid and porphobilinogen in urine
    • Mauzerall, D., and S. Granick. 1956. The occurrence and determination of 5-aminolevulinic acid and porphobilinogen in urine. J. Biol. Chem. 219:435-446.
    • (1956) J. Biol. Chem. , vol.219 , pp. 435-446
    • Mauzerall, D.1    Granick, S.2
  • 20
    • 0027472893 scopus 로고
    • Cloning and characterization of the gene encoding glutamate 1-semialdehyde 2,1-aminomutase, which is involved in δ-aminolevulinic acid synthesis in Propionibacterium freudenreichii
    • Murakami, K., Y. Hashimoto, and Y. Murooka. 1993. Cloning and characterization of the gene encoding glutamate 1-semialdehyde 2,1-aminomutase, which is involved in δ-aminolevulinic acid synthesis in Propionibacterium freudenreichii. Appl. Environ. Microbiol. 59:347-350.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 347-350
    • Murakami, K.1    Hashimoto, Y.2    Murooka, Y.3
  • 21
    • 0027252484 scopus 로고
    • 5-Aminolevulinic acid availability and control of spectral complex formation in HemA and HemT mutants of Rhodobacter sphaeroides
    • Neidle, E. L., and S. Kaplan. 1993. 5-Aminolevulinic acid availability and control of spectral complex formation in HemA and HemT mutants of Rhodobacter sphaeroides. J. Bacteriol. 175:2304-2313.
    • (1993) J. Bacteriol. , vol.175 , pp. 2304-2313
    • Neidle, E.L.1    Kaplan, S.2
  • 22
    • 10444274727 scopus 로고
    • The absorption spectra of porphyrin alpha and derivatives
    • Oliver, I. T., and W. A. Rawlinson. 1955. The absorption spectra of porphyrin alpha and derivatives. Biochem. J. 61:641-646.
    • (1955) Biochem. J. , vol.61 , pp. 641-646
    • Oliver, I.T.1    Rawlinson, W.A.2
  • 23
    • 0015725243 scopus 로고
    • Comparison of porphyrin and heme biosynthesis in various heterotrophic bacteria
    • Philipp-Dormston, W. K., and M. Doss. 1973. Comparison of porphyrin and heme biosynthesis in various heterotrophic bacteria. Enzyme 16:57-64.
    • (1973) Enzyme , vol.16 , pp. 57-64
    • Philipp-Dormston, W.K.1    Doss, M.2
  • 25
    • 0030738625 scopus 로고    scopus 로고
    • Correlation between porphyrin biosynthesis and photodynamic inactivation of Pseudomonas aeruginosa after incubation with 5-aminolaevulinic acid
    • Sailer, R., W. S. L. Strauss, K. Konig, A. Ruck, and R. Steiner. 1997. Correlation between porphyrin biosynthesis and photodynamic inactivation of Pseudomonas aeruginosa after incubation with 5-aminolaevulinic acid. J. Pnotochem. Photobiol. B Biol. 39:236-242.
    • (1997) J. Pnotochem. Photobiol. B Biol. , vol.39 , pp. 236-242
    • Sailer, R.1    Strauss, W.S.L.2    Konig, K.3    Ruck, A.4    Steiner, R.5
  • 27
    • 0020426709 scopus 로고
    • Delta-aminolevulinic acid dehydratase assay
    • Sassa, S. 1982. Delta-aminolevulinic acid dehydratase assay. Enzyme 28:133-145.
    • (1982) Enzyme , vol.28 , pp. 133-145
    • Sassa, S.1
  • 29
    • 0003775317 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Vorobjeva, L. I. 1999. Propionibacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1999) Propionibacteria
    • Vorobjeva, L.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.