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Volumn 370, Issue 2, 2003, Pages 505-516

Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium

Author keywords

CbiX; SirA; SirB; SirC; Sirohydrochlorin

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CHELATION; DEHYDROGENATION; ESCHERICHIA COLI; GENES;

EID: 0037337451     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021443     Document Type: Article
Times cited : (80)

References (35)
  • 2
    • 0030662568 scopus 로고    scopus 로고
    • Mechanism and regulation of Mg-chelatase
    • Walker, C. J. and Willows, R. D. (1997) Mechanism and regulation of Mg-chelatase. Biochem. J. 327, 321-333
    • (1997) Biochem. J. , vol.327 , pp. 321-333
    • Walker, C.J.1    Willows, R.D.2
  • 4
    • 0028278283 scopus 로고
    • Prime time for Bacillus megaterium
    • Vary, P. (1994) Prime time for Bacillus megaterium. Microbiology 140, 1001-1013
    • (1994) Microbiology , vol.140 , pp. 1001-1013
    • Vary, P.1
  • 5
    • 0033560052 scopus 로고    scopus 로고
    • The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and cobalamin biosynthesis
    • Raux, E., McVeigh, T., Peters, S. E., Leustek, T. and Warren, M. J. (1999) The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and cobalamin biosynthesis. Biochem. J. 338, 701-708
    • (1999) Biochem. J. , vol.338 , pp. 701-708
    • Raux, E.1    McVeigh, T.2    Peters, S.E.3    Leustek, T.4    Warren, M.J.5
  • 6
    • 0027497266 scopus 로고
    • The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase
    • Spencer, J. B., Stolowich, N. J., Roessner, C. A. and Scott, A. I. (1993) The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase. FEBS Lett. 335, 57-60
    • (1993) FEBS Lett. , vol.335 , pp. 57-60
    • Spencer, J.B.1    Stolowich, N.J.2    Roessner, C.A.3    Scott, A.I.4
  • 7
    • 0028095384 scopus 로고
    • Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein
    • Warren, M. J., Bolt, E. L., Roessner, C. A., Scott, A. I., Spencer, J. B. and Woodcock, S. C. (1994) Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein. Biochem. J. 302, 837-844
    • (1994) Biochem. J. , vol.302 , pp. 837-844
    • Warren, M.J.1    Bolt, E.L.2    Roessner, C.A.3    Scott, A.I.4    Spencer, J.B.5    Woodcock, S.C.6
  • 8
    • 0031849756 scopus 로고    scopus 로고
    • The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase
    • Schubert, H. L., Wilson, K. S., Raux, E., Woodcock, S. C. and Warren, M. J. (1998) The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. Nat. Struct. Biol. 5, 585-592
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 585-592
    • Schubert, H.L.1    Wilson, K.S.2    Raux, E.3    Woodcock, S.C.4    Warren, M.J.5
  • 9
    • 0036566459 scopus 로고    scopus 로고
    • The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase
    • Schubert, H. L., Raux, E., Brindley, A. A., Leech, H. K., Wilson, K. S., Hill, C. P. and Warren, M. J. (2002) The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. EMBO J. 21, 1-8
    • (2002) EMBO J. , vol.21 , pp. 1-8
    • Schubert, H.L.1    Raux, E.2    Brindley, A.A.3    Leech, H.K.4    Wilson, K.S.5    Hill, C.P.6    Warren, M.J.7
  • 10
    • 0033025509 scopus 로고    scopus 로고
    • Organization of genes for tetrapyrrole biosynthesis in gram-positive bacteria
    • Johansson, P. and Hederstedt, L. (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
  • 11
    • 0032190037 scopus 로고    scopus 로고
    • 12) biosynthesis: Functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide
    • 12) biosynthesis: functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide. Biochem. J. 335, 167-173
    • (1998) Biochem. J. , vol.335 , pp. 167-173
    • Raux, E.1    Lanois, A.2    Rambach, A.3    Warren, M.J.4    Thermes, C.5
  • 12
    • 0032189235 scopus 로고    scopus 로고
    • 12) biosynthesis: Identification and characterization of a Bacillus megaterium cobl operon
    • 12) biosynthesis: identification and characterization of a Bacillus megaterium cobl operon. Biochem. J. 335, 159-166
    • (1998) Biochem. J. , vol.335 , pp. 159-166
    • Raux, E.1    Lanois, A.2    Warren, M.J.3    Rambach, A.4    Thermes, C.5
  • 14
    • 0033578347 scopus 로고    scopus 로고
    • Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis
    • Schubert, H. L., Raux, E., Wilson, K. S. and Warren, M. J. (1999) Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis. Biochemistry 38, 10660-10669
    • (1999) Biochemistry , vol.38 , pp. 10660-10669
    • Schubert, H.L.1    Raux, E.2    Wilson, K.S.3    Warren, M.J.4
  • 16
    • 0025765503 scopus 로고
    • The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III
    • Hansson, M., Rutberg, L., Schroder, I. and Hederstedt, L. (1991) The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III. J. Bacteriol. 173, 2590-2599
    • (1991) J. Bacteriol. , vol.173 , pp. 2590-2599
    • Hansson, M.1    Rutberg, L.2    Schroder, I.3    Hederstedt, L.4
  • 17
    • 0025815889 scopus 로고
    • Primary structure, expression in Escherichia coli, and properties of S-adenosyl-L-methionine: Uroporphyrinogen III methyltransferase from Bacillus megaterium
    • Robin, C., Blanche, F., Cauchois, L., Cameron, B., Couder, M. and Crouzet, J. (1991) Primary structure, expression in Escherichia coli, and properties of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Bacillus megaterium. J. Bacteriol. 173, 4893-4896
    • (1991) J. Bacteriol. , vol.173 , pp. 4893-4896
    • Robin, C.1    Blanche, F.2    Cauchois, L.3    Cameron, B.4    Couder, M.5    Crouzet, J.6
  • 18
    • 0019553597 scopus 로고
    • Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides
    • Jordan, P. M. and Berry, A. (1981) Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides. Biochem. J. 195, 177-181
    • (1981) Biochem. J. , vol.195 , pp. 177-181
    • Jordan, P.M.1    Berry, A.2
  • 19
    • 0024285820 scopus 로고
    • Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase
    • Warren, M. J. and Jordan, P. M. (1988) Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase. Biochemistry 27, 9020-9030
    • (1988) Biochemistry , vol.27 , pp. 9020-9030
    • Warren, M.J.1    Jordan, P.M.2
  • 20
    • 0001794011 scopus 로고
    • The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III
    • Jordan, P. M., ed. Elsevier, Amsterdam
    • Jordan, P. M. (1991) The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III, in 'Biosynthesis of Tetrapyrroles' (Jordan, P. M., ed.), pp. 1-59, Elsevier, Amsterdam
    • (1991) Biosynthesis of Tetrapyrroles , pp. 1-59
    • Jordan, P.M.1
  • 21
    • 0023258705 scopus 로고
    • Lack of redox control of the anaerobicallyinduced nirB+ gene of Escherichia coli K-12
    • Griffiths, L. A. and Cole, J. A. (1987) Lack of redox control of the anaerobicallyinduced nirB+ gene of Escherichia coli K-12. Arch. Microbiol. 147, 364-369
    • (1987) Arch. Microbiol. , vol.147 , pp. 364-369
    • Griffiths, L.A.1    Cole, J.A.2
  • 22
    • 0024720183 scopus 로고
    • Purification and characterization of S-adenosyl-L-methionine: Uroporphyrinogen III methyltransferase from Pseudomonas denitrificans
    • Blanche, F., Debussche, L., Thibaut, D., Crouzet, J. and Cameron, B. (1989) Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans. J. Bacteriol. 171, 4222-4231
    • (1989) J. Bacteriol. , vol.171 , pp. 4222-4231
    • Blanche, F.1    Debussche, L.2    Thibaut, D.3    Crouzet, J.4    Cameron, B.5
  • 23
    • 0025168569 scopus 로고
    • Nucleotide sequence of a Pseudomonas denitrificans 5.4 kb DNA fragment containing five cob genes and identification of structural genes encoding S-adenosyl-L-methionine: Uroporphyrinogen III methyltransferase and cobyrinic acid a,c-diamide synthase
    • Crouzet, J., Cauchois, L., Blanche, F., Debussche, L., Thibaut, D., Rouyez, M. C., Rigault, S., Mayaux, J. F. and Cameron, B. (1990) Nucleotide sequence of a Pseudomonas denitrificans 5.4 kb DNA fragment containing five cob genes and identification of structural genes encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase and cobyrinic acid a,c-diamide synthase. J. Bacteriol. 172, 5968-5979
    • (1990) J. Bacteriol. , vol.172 , pp. 5968-5979
    • Crouzet, J.1    Cauchois, L.2    Blanche, F.3    Debussche, L.4    Thibaut, D.5    Rouyez, M.C.6    Rigault, S.7    Mayaux, J.F.8    Cameron, B.9
  • 24
    • 0025057054 scopus 로고
    • Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase
    • Warren, M. J., Stolowich, N. J., Santander, P. J., Roessner, C. A., Sowa, B. A. and Scott, A. I. (1990) Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase. FEBS Lett. 261, 76-80
    • (1990) FEBS Lett. , vol.261 , pp. 76-80
    • Warren, M.J.1    Stolowich, N.J.2    Santander, P.J.3    Roessner, C.A.4    Sowa, B.A.5    Scott, A.I.6
  • 26
    • 0032552894 scopus 로고    scopus 로고
    • Definition of the redox states of cobalt-precorrinoids: Investigation of the substrate and redox specificity of CbiL from Salmonella typhimurium
    • Spencer, P., Stolowich, N. J., Sumner, L. W. and Scott, A. I. (1998) Definition of the redox states of cobalt-precorrinoids: investigation of the substrate and redox specificity of CbiL from Salmonella typhimurium. Biochemistry 37, 14917-14927
    • (1998) Biochemistry , vol.37 , pp. 14917-14927
    • Spencer, P.1    Stolowich, N.J.2    Sumner, L.W.3    Scott, A.I.4
  • 27
    • 37049098889 scopus 로고
    • Preparation and spectroscopic properties of Co(III)-isobacteriochlorins: Relationship to the cobalt-containing proteins from Desulphovibrio gigas and D. desulphuricans
    • Battersby, A. R. and Sheng, Z.-C. (1982) Preparation and spectroscopic properties of Co(III)-isobacteriochlorins: Relationship to the cobalt-containing proteins from Desulphovibrio gigas and D. desulphuricans. J. Chem. Soc., Chem. Commun., 1393-1394
    • (1982) J. Chem. Soc., Chem. Commun. , pp. 1393-1394
    • Battersby, A.R.1    Sheng, Z.-C.2
  • 30
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregutatory proteins controlling zinc homeostasis
    • Outten, C. E. and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregutatory proteins controlling zinc homeostasis. Science (Washington, D.C.) 292, 2488-2492
    • (2001) Science (Washington, D.C.) , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 31
    • 0028102344 scopus 로고
    • Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis
    • Rey, L., Imperial, J., Palacios, J. M. and Ruiz-Argueso, T. (1994) Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis. J. Bacteriol. 176, 6066-6073
    • (1994) J. Bacteriol. , vol.176 , pp. 6066-6073
    • Rey, L.1    Imperial, J.2    Palacios, J.M.3    Ruiz-Argueso, T.4
  • 32
    • 0028911174 scopus 로고
    • HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer
    • Fu, C., Olson, J. W. and Maier, R. J. (1995) HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer. Proc. Natl. Acad. Sci. U.S.A. 92, 2333-2337
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2333-2337
    • Fu, C.1    Olson, J.W.2    Maier, R.J.3
  • 33
    • 0030944159 scopus 로고    scopus 로고
    • In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: Molecular and physiological characterization of cooCTJ
    • Kerby, R. L., Ludden, P. W. and Roberts, G. P. (1997) In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of cooCTJ. J. Bacteriol. 179, 2259-2266
    • (1997) J. Bacteriol. , vol.179 , pp. 2259-2266
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 34
    • 0030612325 scopus 로고    scopus 로고
    • The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase
    • Olson, J. W., Fu, C. and Maier, R. J. (1997) The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase. Mol. Microbiol. 24, 119-128
    • (1997) Mol. Microbiol. , vol.24 , pp. 119-128
    • Olson, J.W.1    Fu, C.2    Maier, R.J.3
  • 35
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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