메뉴 건너뛰기




Volumn 54, Issue 1, 2010, Pages 267-272

Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin

Author keywords

[No Author keywords available]

Indexed keywords

5 ACETAMIDO 4 OXO 5 HEXENOIC ACID; ALAREMYCIN; AMINO ACID; AMINOCAPROIC ACID DERIVATIVE; ANTIBIOTIC AGENT; HEME; LYSINE; PORPHOBILINOGEN SYNTHASE; UNCLASSIFIED DRUG;

EID: 73849132820     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00553-09     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0001006142 scopus 로고
    • Effect of gabaculine on the synthesis of heme and cytochrome f in etiolated wheat seedlings
    • Anderson, C. M., and J. C. Gray. 1991. Effect of gabaculine on the synthesis of heme and cytochrome f in etiolated wheat seedlings. Plant Physiol. 96:584-587.
    • (1991) Plant Physiol , vol.96 , pp. 584-587
    • Anderson, C.M.1    Gray, J.C.2
  • 2
    • 25844472165 scopus 로고    scopus 로고
    • Isolation of a new antibiotic, alaremycin, structurally related to 5-aminolevulinic acid from Streptomyces sp. A012304
    • Awa, Y., N. Iwai, T. Ueda, K. Suzuki, S. Asano, J. Yamagishi, K. Nagai, and M. Wachi. 2005. Isolation of a new antibiotic, alaremycin, structurally related to 5-aminolevulinic acid from Streptomyces sp. A012304. Biosci. Biotechnol. Biochem. 69:1721-1725.
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1721-1725
    • Awa, Y.1    Iwai, N.2    Ueda, T.3    Suzuki, K.4    Asano, S.5    Yamagishi, J.6    Nagai, K.7    Wachi, M.8
  • 3
    • 0028911711 scopus 로고
    • Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barkeri
    • Bhosale, S., D. Kshirsagar, P. Pawar, T. Yeole, and D. Ranade. 1995. Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barkeri. FEMS Microbiol. Lett. 127:151-155.
    • (1995) FEMS Microbiol. Lett , vol.127 , pp. 151-155
    • Bhosale, S.1    Kshirsagar, D.2    Pawar, P.3    Yeole, T.4    Ranade, D.5
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 10
    • 0345281626 scopus 로고    scopus 로고
    • 2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa
    • 2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa. Biochemistry 38:13968-13975.
    • (1999) Biochemistry , vol.38 , pp. 13968-13975
    • Frankenberg, N.1    Heinz, D.W.2    Jahn, D.3
  • 11
    • 0344035680 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions
    • Frankenberg, N., D. Jahn, and E. K. Jaffe. 1999. Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions. Biochemistry 38:13976-13982.
    • (1999) Biochemistry , vol.38 , pp. 13976-13982
    • Frankenberg, N.1    Jahn, D.2    Jaffe, E.K.3
  • 12
    • 33745844831 scopus 로고    scopus 로고
    • Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors
    • Frere, F., M. Nentwich, S. Gacond, D. W. Heinz, R. Neier, and N. Frankenberg-Dinkel. 2006. Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors. Biochemistry 45:8243-8253.
    • (2006) Biochemistry , vol.45 , pp. 8243-8253
    • Frere, F.1    Nentwich, M.2    Gacond, S.3    Heinz, D.W.4    Neier, R.5    Frankenberg-Dinkel, N.6
  • 13
    • 11844251357 scopus 로고    scopus 로고
    • Tracking the evolution of porphobilinogen synthase metal dependence in vitro
    • Frere, F., H. Reents, W. D. Schubert, D. W. Heinz, and D. Jahn. 2005. Tracking the evolution of porphobilinogen synthase metal dependence in vitro. J. Mol. Biol. 345:1059-1070.
    • (2005) J. Mol. Biol , vol.345 , pp. 1059-1070
    • Frere, F.1    Reents, H.2    Schubert, W.D.3    Heinz, D.W.4    Jahn, D.5
  • 14
    • 0036299038 scopus 로고    scopus 로고
    • Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism
    • Frere, F., W. D. Schubert, F. Stauffer, N. Frankenberg, R. Neier, D. Jahn, and D. W. Heinz. 2002. Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism. J. Mol. Biol. 320:237-247.
    • (2002) J. Mol. Biol , vol.320 , pp. 237-247
    • Frere, F.1    Schubert, W.D.2    Stauffer, F.3    Frankenberg, N.4    Neier, R.5    Jahn, D.6    Heinz, D.W.7
  • 17
    • 0037254874 scopus 로고    scopus 로고
    • Investigations on the metal switch region of human porphobilinogen synthase
    • Jaffe, E. K. 2003. Investigations on the metal switch region of human porphobilinogen synthase. J. Biol. Inorg. Chem. 8:176-184.
    • (2003) J. Biol. Inorg. Chem , vol.8 , pp. 176-184
    • Jaffe, E.K.1
  • 18
    • 4644261553 scopus 로고    scopus 로고
    • The porphobilinogen synthase catalyzed reaction mechanism
    • Jaffe, E. K. 2004. The porphobilinogen synthase catalyzed reaction mechanism. Bioorg. Chem. 32:316-325.
    • (2004) Bioorg. Chem , vol.32 , pp. 316-325
    • Jaffe, E.K.1
  • 19
    • 44549088842 scopus 로고
    • Gabaculine inhibition of chlorophyll biosynthesis and nodulation in Phaseolus lunatus L
    • May, T. B., J. A. Guikema, R. L. Henry, M. K. Schuler, and P. P. Wong. 1987. Gabaculine inhibition of chlorophyll biosynthesis and nodulation in Phaseolus lunatus L. Plant Physiol. 84:1309-1313.
    • (1987) Plant Physiol , vol.84 , pp. 1309-1313
    • May, T.B.1    Guikema, J.A.2    Henry, R.L.3    Schuler, M.K.4    Wong, P.P.5
  • 20
    • 0018287635 scopus 로고
    • Mutants of Escherichia coli K12 permeable to haemin
    • McConville, M. L., and H. P. Charles. 1979. Mutants of Escherichia coli K12 permeable to haemin. J. Gen. Microbiol. 113:165-168.
    • (1979) J. Gen. Microbiol , vol.113 , pp. 165-168
    • McConville, M.L.1    Charles, H.P.2
  • 21
    • 73849139328 scopus 로고    scopus 로고
    • Miller, J. H. 1992. A short course in bacterial genetics. A laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Miller, J. H. 1992. A short course in bacterial genetics. A laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0034708125 scopus 로고    scopus 로고
    • Heme metabolism of Plasmodium is a major antimalarial target
    • Padmanaban, G., and P. N. Rangarajan. 2000. Heme metabolism of Plasmodium is a major antimalarial target. Biochem. Biophys. Res. Commun. 268:665-668.
    • (2000) Biochem. Biophys. Res. Commun , vol.268 , pp. 665-668
    • Padmanaban, G.1    Rangarajan, P.N.2
  • 25
    • 33745887481 scopus 로고    scopus 로고
    • Occurrence of two 5-aminolevulinate biosynthetic pathways in Streptomyces nodosus subsp. asukaensis is linked with the production of asukamycin
    • Petricek, M., K. Petrickova, L. Havlicek, and J. Felsberg. 2006. Occurrence of two 5-aminolevulinate biosynthetic pathways in Streptomyces nodosus subsp. asukaensis is linked with the production of asukamycin. J. Bacteriol. 188:5113-5123.
    • (2006) J. Bacteriol , vol.188 , pp. 5113-5123
    • Petricek, M.1    Petrickova, K.2    Havlicek, L.3    Felsberg, J.4
  • 26
    • 0001571980 scopus 로고
    • Delta-aminolevulinic acid, its role in the biosynthesis of porphyrins and purins
    • Shemin, D., and C. S. Russel. 1953. Delta-aminolevulinic acid, its role in the biosynthesis of porphyrins and purins. J. Am. Chem. Soc. 75:4873-4875.
    • (1953) J. Am. Chem. Soc , vol.75 , pp. 4873-4875
    • Shemin, D.1    Russel, C.S.2
  • 28
    • 0024724030 scopus 로고
    • Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene
    • Verkamp, E., and B. K. Chelm. 1989. Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene. J. Bacteriol. 171:4728-4735.
    • (1989) J. Bacteriol , vol.171 , pp. 4728-4735
    • Verkamp, E.1    Chelm, B.K.2
  • 29
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: The role of heme, hemoprotein receptors and hemophores
    • Wandersman, C., and I. Stojiljkovic. 2000. Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr. Opin. Microbiol. 3:215-220.
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.