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Volumn 199, Issue 4, 1996, Pages 557-564

Subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in higher plants: An immunological investigation

Author keywords

Arabidopsis; Chlorophyll biosynthesis; Plastid; Porphobilinogen deaminase (purification, subcellular location)

Indexed keywords

ANIMALIA; ARABIDOPSIS; ARABIDOPSIS THALIANA; EMBRYOPHYTA; ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

EID: 0029840277     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00195187     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 0022338208 scopus 로고
    • ATG vectors for regulated high-level expression of cloned genes in Escherichia coli
    • Amann E, Brosius J (1985) ATG vectors for regulated high-level expression of cloned genes in Escherichia coli. Gene 40: 183-190
    • (1985) Gene , vol.40 , pp. 183-190
    • Amann, E.1    Brosius, J.2
  • 2
    • 0000870242 scopus 로고
    • Leghemoglobin and Rhizobium respiration
    • Appleby CA (1984) Leghemoglobin and Rhizobium respiration. Annu Rev Plant Physiol 35: 443-478
    • (1984) Annu Rev Plant Physiol , vol.35 , pp. 443-478
    • Appleby, C.A.1
  • 3
    • 37049121477 scopus 로고
    • Stereochemistry of biosynthesis of the vinyl group of protoporphyrin IX: A short synthesis of porphobilinogen
    • Battersby AR, McDonald E, Wurzinger HKW, James KJ (1975) Stereochemistry of biosynthesis of the vinyl group of protoporphyrin IX: a short synthesis of porphobilinogen. J Chem Soc Chem Commun 493-495
    • (1975) J Chem Soc Chem Commun , pp. 493-495
    • Battersby, A.R.1    McDonald, E.2    Wurzinger, H.K.W.3    James, K.J.4
  • 4
    • 37049108452 scopus 로고
    • Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and the substrate for cosynthetase in the biosynthesis of uroporphyrinogen III
    • Battersby AR, Fookes CJR, Gustafson-Potter K, Matcham GWJ, McDonald E (1979) Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and the substrate for cosynthetase in the biosynthesis of uroporphyrinogen III. J Chem Soc Chem Commun 1155-1158
    • (1979) J Chem Soc Chem Commun , pp. 1155-1158
    • Battersby, A.R.1    Fookes, C.J.R.2    Gustafson-Potter, K.3    Matcham, G.W.J.4    McDonald, E.5
  • 5
    • 0011116090 scopus 로고
    • Acquired disorders of haem synthesis
    • Elder GH (1976) Acquired disorders of haem synthesis. Essays Med Biochem 2: 75-114
    • (1976) Essays Med Biochem , vol.2 , pp. 75-114
    • Elder, G.H.1
  • 6
    • 37049075825 scopus 로고
    • Biosynthesis of the natural porphyrins: Proof that hydroxymethylbilane synthase (porphobilinogen deaminase) uses a novel binding group in its catalytic action
    • Hart GJ, Miller AD, Leeper FJ, Battersby AR (1987) Biosynthesis of the natural porphyrins: proof that hydroxymethylbilane synthase (porphobilinogen deaminase) uses a novel binding group in its catalytic action. J Chem Soc Chem Comm 1762-1765
    • (1987) J Chem Soc Chem Comm , pp. 1762-1765
    • Hart, G.J.1    Miller, A.D.2    Leeper, F.J.3    Battersby, A.R.4
  • 7
    • 0001164098 scopus 로고
    • Porphyrin accumulation and export by isolated barley (Hordeum vulgari) plastids effect of diphenylether herbicides
    • Jacobs JM, Jacobs NJ (1993) Porphyrin accumulation and export by isolated barley (Hordeum vulgari) plastids effect of diphenylether herbicides. Plant Physiol 101: 1181-1187
    • (1993) Plant Physiol , vol.101 , pp. 1181-1187
    • Jacobs, J.M.1    Jacobs, N.J.2
  • 8
    • 0028198439 scopus 로고
    • Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana
    • Jones RM, Jordan PM (1994) Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana. Biochem J 299: 895-902
    • (1994) Biochem J , vol.299 , pp. 895-902
    • Jones, R.M.1    Jordan, P.M.2
  • 9
    • 0001794011 scopus 로고
    • The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III
    • Jordan PM (ed) Elsevier, Amsterdam
    • Jordan PM (1991) The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III. In: Jordan PM (ed) Biosynthesis of tetrapyrroles. Elsevier, Amsterdam, pp 1-59
    • (1991) Biosynthesis of Tetrapyrroles , pp. 1-59
    • Jordan, P.M.1
  • 10
    • 0022559019 scopus 로고
    • Purification of porphobilinogen synthase from bovine liver
    • Jordan PM, Seehra JS (1986) Purification of porphobilinogen synthase from bovine liver. Methods Enzymol 123: 427-434
    • (1986) Methods Enzymol , vol.123 , pp. 427-434
    • Jordan, P.M.1    Seehra, J.S.2
  • 11
    • 0023650414 scopus 로고
    • Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase
    • Jordan PM, Warren MJ (1987) Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase. FEBS Lett 225: 87-92
    • (1987) FEBS Lett , vol.225 , pp. 87-92
    • Jordan, P.M.1    Warren, M.J.2
  • 12
    • 0026045161 scopus 로고
    • Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation
    • Jordan PM, Woodcock SC (1991) Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. Biochem J 280: 445-449
    • (1991) Biochem J , vol.280 , pp. 445-449
    • Jordan, P.M.1    Woodcock, S.C.2
  • 14
    • 0023678482 scopus 로고
    • Identification of a cysteine residue as the binding-site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase
    • Jordan PM, Warren MJ, Williams HJ, Stolowich NJ, Roessner CA, Grant SK, Scott AI (1988) Identification of a cysteine residue as the binding-site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase. FEBS Lett 235: 189-193
    • (1988) FEBS Lett , vol.235 , pp. 189-193
    • Jordan, P.M.1    Warren, M.J.2    Williams, H.J.3    Stolowich, N.J.4    Roessner, C.A.5    Grant, S.K.6    Scott, A.I.7
  • 15
    • 0023553698 scopus 로고
    • Processing of a wheat light-harvesting chlorophyll a/b protein-precursor by a soluble enzyme from higher plant chloroplasts
    • Lamppa GK, Abad MS (1987) Processing of a wheat light-harvesting chlorophyll a/b protein-precursor by a soluble enzyme from higher plant chloroplasts. J Cell Biol 105: 2641-2648
    • (1987) J Cell Biol , vol.105 , pp. 2641-2648
    • Lamppa, G.K.1    Abad, M.S.2
  • 16
    • 0028534598 scopus 로고
    • Porphobilinogen deaminase is encoded by a single gene in Arabidopsis thaliana and is targeted to the chloroplasts
    • Lim SH, Witty M, Wallace-Cook ADM, Ilag LI, Smith AG (1994) Porphobilinogen deaminase is encoded by a single gene in Arabidopsis thaliana and is targeted to the chloroplasts. Plant Mol Biol 26: 863-872
    • (1994) Plant Mol Biol , vol.26 , pp. 863-872
    • Lim, S.H.1    Witty, M.2    Wallace-Cook, A.D.M.3    Ilag, L.I.4    Smith, A.G.5
  • 18
    • 0027673660 scopus 로고
    • A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules
    • Madsen O, Sandal L, Sandal NN, Marcker KA (1993) A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules. Plant Mol Biol 23: 35-43
    • (1993) Plant Mol Biol , vol.23 , pp. 35-43
    • Madsen, O.1    Sandal, L.2    Sandal, N.N.3    Marcker, K.A.4
  • 19
    • 0023688529 scopus 로고
    • Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulfur atom of cysteine-242
    • Miller A, Hart GJ, Packman LC, Battersby AR (1988) Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulfur atom of cysteine-242. Biochem J 254: 915-918
    • (1988) Biochem J , vol.254 , pp. 915-918
    • Miller, A.1    Hart, G.J.2    Packman, L.C.3    Battersby, A.R.4
  • 20
    • 0014961134 scopus 로고
    • A dipyrrylmethane intermediate in the enzymic synthesis of uroporphyrinogen
    • Pluscec J, Bogorad L (1970) A dipyrrylmethane intermediate in the enzymic synthesis of uroporphyrinogen. Biochemistry 9: 4736-4743
    • (1970) Biochemistry , vol.9 , pp. 4736-4743
    • Pluscec, J.1    Bogorad, L.2
  • 22
    • 0024971353 scopus 로고
    • Isolation and characterization of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis
    • Sharif AL, Smith AG, Abell C (1989) Isolation and characterization of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis. Eur J Biochem 184: 353-359
    • (1989) Eur J Biochem , vol.184 , pp. 353-359
    • Sharif, A.L.1    Smith, A.G.2    Abell, C.3
  • 23
    • 0024286451 scopus 로고
    • Subcellular localization of two porphyrin-synthesis enzymes in Pisum satvum (pea) and Arum (cuckoo-pint) species
    • Smith AG (1988) Subcellular localization of two porphyrin-synthesis enzymes in Pisum satvum (pea) and Arum (cuckoo-pint) species. Biochem J 249: 423-428
    • (1988) Biochem J , vol.249 , pp. 423-428
    • Smith, A.G.1
  • 24
    • 0027213464 scopus 로고
    • Investigation of the subcellular location of the tetrapyrrole biosynthesis enzyme coproporphyrinogen oxidase in higher plants
    • Smith AG, Marsh O, Elder GH (1993) Investigation of the subcellular location of the tetrapyrrole biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem J 292: 503-508
    • (1993) Biochem J , vol.292 , pp. 503-508
    • Smith, A.G.1    Marsh, O.2    Elder, G.H.3
  • 25
    • 0023046907 scopus 로고
    • Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12
    • Thomas SD, Jordan PM (1986) Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. Nucleic Acids Res 14: 6215-6226
    • (1986) Nucleic Acids Res , vol.14 , pp. 6215-6226
    • Thomas, S.D.1    Jordan, P.M.2
  • 26
    • 0024286687 scopus 로고
    • Haem synthesis during cytochrome P-450 induction in higher plants
    • Werck-Reichhart D, Jones OTG, Durst F (1988) Haem synthesis during cytochrome P-450 induction in higher plants. Biochem J 249: 473-480
    • (1988) Biochem J , vol.249 , pp. 473-480
    • Werck-Reichhart, D.1    Jones, O.T.G.2    Durst, F.3
  • 27
    • 0019395899 scopus 로고
    • Purification of porphobilinogen deaminase from Eugleina gracilis and studies of its kinetics
    • Williams DC, Morgan GS, McDonald E, Battersby AR (1981) Purification of porphobilinogen deaminase from Eugleina gracilis and studies of its kinetics. Biochem J 193: 301-310
    • (1981) Biochem J , vol.193 , pp. 301-310
    • Williams, D.C.1    Morgan, G.S.2    McDonald, E.3    Battersby, A.R.4
  • 28
    • 0027667070 scopus 로고
    • Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction
    • Witty M, Wallace-Cook ADM, Albrecht H, Spano AJ, Michel H, Shabanowitz J, Hunt DF, Timko MP, Smith AG (1993) Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction. Plant Physiol 103: 139-147
    • (1993) Plant Physiol , vol.103 , pp. 139-147
    • Witty, M.1    Wallace-Cook, A.D.M.2    Albrecht, H.3    Spano, A.J.4    Michel, H.5    Shabanowitz, J.6    Hunt, D.F.7    Timko, M.P.8    Smith, A.G.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.