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Volumn 12, Issue 2, 2008, Pages 118-125

Cofactor biosynthesis-still yielding fascinating new biological chemistry

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; ENZYME; MOLYBDOPTERIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PORPHYRIN; PYRIDOXAL 5 PHOSPHATE; PYRIMIDINE; THIAMINE; THIAZOLE;

EID: 43049116428     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.02.006     Document Type: Review
Times cited : (35)

References (34)
  • 1
    • 34247514313 scopus 로고    scopus 로고
    • Thiamin phosphate synthase: the rate of pyrimidine carbocation formation
    • Structural and kinetic characterization of the pyrimidine carbocation intermediate generated at the active site of thiamin phosphate synthase.
    • Hanes J.W., Ealick S.E., and Begley T.P. Thiamin phosphate synthase: the rate of pyrimidine carbocation formation. J Am Chem Soc 129 (2007) 4860-4861. Structural and kinetic characterization of the pyrimidine carbocation intermediate generated at the active site of thiamin phosphate synthase.
    • (2007) J Am Chem Soc , vol.129 , pp. 4860-4861
    • Hanes, J.W.1    Ealick, S.E.2    Begley, T.P.3
  • 2
    • 33746265805 scopus 로고    scopus 로고
    • Biosynthesis of thiamin thiazole: determination of the regiochemistry of the S/O acyl shift by using 1,4-dideoxy-d-xylulose-5-phosphate
    • Determination that the acyl shift in thiamin thiazole biosynthesis occurs to the C3 hydroxyl of DXP.
    • Chatterjee A., Han X., McLafferty F.W., and Begley T.P. Biosynthesis of thiamin thiazole: determination of the regiochemistry of the S/O acyl shift by using 1,4-dideoxy-d-xylulose-5-phosphate. Angew Chem Int Ed 45 (2006) 3507-3510. Determination that the acyl shift in thiamin thiazole biosynthesis occurs to the C3 hydroxyl of DXP.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 3507-3510
    • Chatterjee, A.1    Han, X.2    McLafferty, F.W.3    Begley, T.P.4
  • 3
    • 5444256191 scopus 로고    scopus 로고
    • The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS
    • Mechanistic characterization of the bacterial thiazole synthase.
    • Dorrestein P.C., Zhai H., McLafferty F.W., and Begley T.P. The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS. Chem Biol 11 (2004) 1373-1381. Mechanistic characterization of the bacterial thiazole synthase.
    • (2004) Chem Biol , vol.11 , pp. 1373-1381
    • Dorrestein, P.C.1    Zhai, H.2    McLafferty, F.W.3    Begley, T.P.4
  • 4
    • 1642407640 scopus 로고    scopus 로고
    • The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase
    • Mechanistic characterization of the early steps in bacterial thiazole biosynthesis.
    • Dorrestein P.C., Zhai H., Taylor S.V., McLafferty F.W., and Begley T.P. The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase. J Am Chem Soc 126 (2004) 3091-3096. Mechanistic characterization of the early steps in bacterial thiazole biosynthesis.
    • (2004) J Am Chem Soc , vol.126 , pp. 3091-3096
    • Dorrestein, P.C.1    Zhai, H.2    Taylor, S.V.3    McLafferty, F.W.4    Begley, T.P.5
  • 5
    • 19444371837 scopus 로고    scopus 로고
    • Structural analysis of Escherichia coli ThiF
    • The structure of the enzyme involved in the activation of the sulfur carrier protein involved in thiazole biosynthesis.
    • Duda D.M., Walden H., Sfondouris J., and Schulman B.A. Structural analysis of Escherichia coli ThiF. J Mol Biol 349 (2005) 774-786. The structure of the enzyme involved in the activation of the sulfur carrier protein involved in thiazole biosynthesis.
    • (2005) J Mol Biol , vol.349 , pp. 774-786
    • Duda, D.M.1    Walden, H.2    Sfondouris, J.3    Schulman, B.A.4
  • 6
    • 30144434909 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ThiS-ThiFcomplex, a key component of the sulfur transfer system in thiamin biosynthesis
    • The structure of the ThiF-ThiS complex involved in sulfur transfer from cysteine to the thiamin thiazole.
    • Lehmann C., Begley T.P., and Ealick S.E. Structure of the Escherichia coli ThiS-ThiFcomplex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45 (2006) 11-19. The structure of the ThiF-ThiS complex involved in sulfur transfer from cysteine to the thiamin thiazole.
    • (2006) Biochemistry , vol.45 , pp. 11-19
    • Lehmann, C.1    Begley, T.P.2    Ealick, S.E.3
  • 7
    • 0142126717 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)
    • Reconstitution of bacterial thiazole biosynthesis in a biochemically defined system.
    • Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W., and Begley T.P. Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1). Biochemistry 42 (2003) 12430-12438. Reconstitution of bacterial thiazole biosynthesis in a biochemically defined system.
    • (2003) Biochemistry , vol.42 , pp. 12430-12438
    • Park, J.-H.1    Dorrestein, P.C.2    Zhai, H.3    Kinsland, C.4    McLafferty, F.W.5    Begley, T.P.6
  • 8
    • 4644350111 scopus 로고    scopus 로고
    • Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex
    • Structural characterization of the bacterial thiazole synthase reveals a simple active site catalyzing a complex reaction.
    • Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., McLafferty F.W., Begley T.P., and Ealick S.E. Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex. Biochemistry 43 (2004) 11647-11657. Structural characterization of the bacterial thiazole synthase reveals a simple active site catalyzing a complex reaction.
    • (2004) Biochemistry , vol.43 , pp. 11647-11657
    • Settembre, E.C.1    Dorrestein, P.C.2    Zhai, H.3    Chatterjee, A.4    McLafferty, F.W.5    Begley, T.P.6    Ealick, S.E.7
  • 9
    • 0037452907 scopus 로고    scopus 로고
    • Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis
    • Structural studies on ThiO support a hydride transfer mechanism.
    • Settembre E.C., Dorrestein P.C., Park J.-H., Augustine A.M., Begley T.P., and Ealick S.E. Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry 42 (2003) 2971-2981. Structural studies on ThiO support a hydride transfer mechanism.
    • (2003) Biochemistry , vol.42 , pp. 2971-2981
    • Settembre, E.C.1    Dorrestein, P.C.2    Park, J.-H.3    Augustine, A.M.4    Begley, T.P.5    Ealick, S.E.6
  • 10
    • 34547107087 scopus 로고    scopus 로고
    • Thiazole synthase from Escherichia coli: an investigation of the substates and purified proteins required for activity in vitro
    • Reconstitution of the ThiH-dependent thiazole biosynthesis and the identification that ThiH is a radical SAM enzyme.
    • Kriek M., Martins F., Leonardi R., Fairhurst S.A., Lowe D.J., and Roach P.L. Thiazole synthase from Escherichia coli: an investigation of the substates and purified proteins required for activity in vitro. J Biol Chem 282 (2007) 17413-17423. Reconstitution of the ThiH-dependent thiazole biosynthesis and the identification that ThiH is a radical SAM enzyme.
    • (2007) J Biol Chem , vol.282 , pp. 17413-17423
    • Kriek, M.1    Martins, F.2    Leonardi, R.3    Fairhurst, S.A.4    Lowe, D.J.5    Roach, P.L.6
  • 11
    • 4744361651 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction
    • Reconstitution of the remarkable conversion of 5-aminoimidazole ribonucleotide to the thiamin pyrimidine.
    • Lawhorn B.G., Mehl R.A., and Begley T.P. Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction. Org Biomol Chem 2 (2004) 2538-2546. Reconstitution of the remarkable conversion of 5-aminoimidazole ribonucleotide to the thiamin pyrimidine.
    • (2004) Org Biomol Chem , vol.2 , pp. 2538-2546
    • Lawhorn, B.G.1    Mehl, R.A.2    Begley, T.P.3
  • 12
    • 33947204418 scopus 로고    scopus 로고
    • Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate
    • Demonstration that the thiamin thiazole in eukaryotes is derived from NAD.
    • Chatterjee A., Jurgenson C.T., Schroeder F.C., Ealick S.E., and Begley T.P. Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate. J Am Chem Soc 129 (2007) 2914-2922. Demonstration that the thiamin thiazole in eukaryotes is derived from NAD.
    • (2007) J Am Chem Soc , vol.129 , pp. 2914-2922
    • Chatterjee, A.1    Jurgenson, C.T.2    Schroeder, F.C.3    Ealick, S.E.4    Begley, T.P.5
  • 13
    • 33748803376 scopus 로고    scopus 로고
    • Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae
    • Structural studies on the eukaryotic thiazole synthase from Saccharomyces cerevisiae showing bound ADP-thiazole.
    • Jurgenson C.T., Chatterjee A., Begley T.P., and Ealick S.E. Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae. Biochemistry 45 (2006) 11061-11070. Structural studies on the eukaryotic thiazole synthase from Saccharomyces cerevisiae showing bound ADP-thiazole.
    • (2006) Biochemistry , vol.45 , pp. 11061-11070
    • Jurgenson, C.T.1    Chatterjee, A.2    Begley, T.P.3    Ealick, S.E.4
  • 14
    • 33744932425 scopus 로고    scopus 로고
    • Thiamin biosynthesis in eukaryotes: characterization of the enzyme-bound product of thiazole synthase from Saccharomyces cerevisiae and its implications in thiazole biosynthesis
    • The identification of a Thi4-bound metabolite reveals the function of the eukaryotic thiazole synthase.
    • Chatterjee A., Jurgenson C.T., Schroeder F.C., Ealick S.E., and Begley T.P. Thiamin biosynthesis in eukaryotes: characterization of the enzyme-bound product of thiazole synthase from Saccharomyces cerevisiae and its implications in thiazole biosynthesis. J Am Chem Soc 128 (2006) 7158-7159. The identification of a Thi4-bound metabolite reveals the function of the eukaryotic thiazole synthase.
    • (2006) J Am Chem Soc , vol.128 , pp. 7158-7159
    • Chatterjee, A.1    Jurgenson, C.T.2    Schroeder, F.C.3    Ealick, S.E.4    Begley, T.P.5
  • 15
    • 33750054105 scopus 로고    scopus 로고
    • Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana
    • Structural studies on the eukaryotic thiazole synthase from Arabidopsis thaliana showing bound ADP-thiazole.
    • Godoi P.H.C., Galhardo R.S., Luche D.D., Van Sluys M.-A., Menck C.F.M., and Oliva G. Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana. J Biol Chem 281 (2006) 30957-30966. Structural studies on the eukaryotic thiazole synthase from Arabidopsis thaliana showing bound ADP-thiazole.
    • (2006) J Biol Chem , vol.281 , pp. 30957-30966
    • Godoi, P.H.C.1    Galhardo, R.S.2    Luche, D.D.3    Van Sluys, M.-A.4    Menck, C.F.M.5    Oliva, G.6
  • 16
    • 0142183433 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid
    • Isotopic labeling studies demonstrate that the pyrimidine moiety of thiamin in S. cerevisiae is derived from histidine and PLP.
    • Zeidler J., Sayer B.G., and Spenser I.D. Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid. J Am Chem Soc 125 (2003) 13094-13105. Isotopic labeling studies demonstrate that the pyrimidine moiety of thiamin in S. cerevisiae is derived from histidine and PLP.
    • (2003) J Am Chem Soc , vol.125 , pp. 13094-13105
    • Zeidler, J.1    Sayer, B.G.2    Spenser, I.D.3
  • 17
    • 34447518986 scopus 로고    scopus 로고
    • A new thiamin salvage pathway
    • Functional studies on TenA lead to a new thiamin salvage pathway.
    • Jenkins A.H., Schyns G., Potot S., Sun G., and Begley T.P. A new thiamin salvage pathway. Nat Chem Biol 3 (2007) 492-497. Functional studies on TenA lead to a new thiamin salvage pathway.
    • (2007) Nat Chem Biol , vol.3 , pp. 492-497
    • Jenkins, A.H.1    Schyns, G.2    Potot, S.3    Sun, G.4    Begley, T.P.5
  • 18
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
    • Structural studies on MoaA, an intriguing enzyme catalyzing a new rearrangement of GTP.
    • Hanzelmann P., and Schindelin H. Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. Proc Natl Acad Sci 103 (2006) 6829-6834. Structural studies on MoaA, an intriguing enzyme catalyzing a new rearrangement of GTP.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 6829-6834
    • Hanzelmann, P.1    Schindelin, H.2
  • 19
    • 0037226754 scopus 로고    scopus 로고
    • Mechanism and structure of biosynthetic enzymes. The biosynthesis of vitamin B6
    • A review describing the current status of our understanding of the E. coli PLP biosynthetic pathway.
    • Cane D.E. Mechanism and structure of biosynthetic enzymes. The biosynthesis of vitamin B6. Chimia 57 (2003) 75-76. A review describing the current status of our understanding of the E. coli PLP biosynthetic pathway.
    • (2003) Chimia , vol.57 , pp. 75-76
    • Cane, D.E.1
  • 20
    • 0033529936 scopus 로고    scopus 로고
    • A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis
    • A major contribution pointing toward a new PLP biosynthetic pathway based on singlet oxygen resistance.
    • Ehrenshaft M., Bilski P., Li M.Y., Chignell C.F., and Daub M.E. A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. Proc Natl Acad Sci 96 (1999) 9374-9378. A major contribution pointing toward a new PLP biosynthetic pathway based on singlet oxygen resistance.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 9374-9378
    • Ehrenshaft, M.1    Bilski, P.2    Li, M.Y.3    Chignell, C.F.4    Daub, M.E.5
  • 21
    • 34250350465 scopus 로고    scopus 로고
    • Reaction mechanism of pyridoxal 5′-phosphate synthase: detection of an enzyme-bound chromophoric intermediate
    • Mechanistic analysis of the DXP-independent PLP synthase.
    • Raschle T., Arigoni D., Brunisholz R., Rechsteiner H., Amrhein N., and Fitzpatrick T.B. Reaction mechanism of pyridoxal 5′-phosphate synthase: detection of an enzyme-bound chromophoric intermediate. J Biol Chem 282 (2007) 6098-6105. Mechanistic analysis of the DXP-independent PLP synthase.
    • (2007) J Biol Chem , vol.282 , pp. 6098-6105
    • Raschle, T.1    Arigoni, D.2    Brunisholz, R.3    Rechsteiner, H.4    Amrhein, N.5    Fitzpatrick, T.B.6
  • 22
    • 33845928807 scopus 로고    scopus 로고
    • Structure of a bacterial pyridoxal 5′-phosphate synthase complex
    • Structural studies on the DXP-independent PLP synthase.
    • Strohmeier M., Raschle T., Mazurkiewicz J., Rippe K., Sinning I., Fitzpatrick T.B., and Tews I. Structure of a bacterial pyridoxal 5′-phosphate synthase complex. Proc Natl Acad Sci U S A 103 (2006) 19284-19289. Structural studies on the DXP-independent PLP synthase.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19284-19289
    • Strohmeier, M.1    Raschle, T.2    Mazurkiewicz, J.3    Rippe, K.4    Sinning, I.5    Fitzpatrick, T.B.6    Tews, I.7
  • 23
    • 33845468647 scopus 로고    scopus 로고
    • Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima
    • Structural studies on the DXP-independent PLP synthase.
    • Zein F., Zhang Y., Kang Y.-N., Burns K., Begley T.P., and Ealick S.E. Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry 45 (2006) 14609-14620. Structural studies on the DXP-independent PLP synthase.
    • (2006) Biochemistry , vol.45 , pp. 14609-14620
    • Zein, F.1    Zhang, Y.2    Kang, Y.-N.3    Burns, K.4    Begley, T.P.5    Ealick, S.E.6
  • 24
    • 15744377644 scopus 로고    scopus 로고
    • Reconstitution and biochemical characterization of a new pyridoxal-5′-phosphate biosynthetic pathway
    • Reconstitution of PLP biosynthesis by the DXP-independent pathway.
    • Burns K.E., Xiang Y., Kinsland C.L., McLafferty F.W., and Begley T.P. Reconstitution and biochemical characterization of a new pyridoxal-5′-phosphate biosynthetic pathway. J Am Chem Soc 127 (2005) 3682-3683. Reconstitution of PLP biosynthesis by the DXP-independent pathway.
    • (2005) J Am Chem Soc , vol.127 , pp. 3682-3683
    • Burns, K.E.1    Xiang, Y.2    Kinsland, C.L.3    McLafferty, F.W.4    Begley, T.P.5
  • 25
    • 41449108267 scopus 로고    scopus 로고
    • Hanes JW, Burns KE, Hilmey DG, Chatterjee A, Dorrestein PC, Begley TP: Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway leading to a chromophoric intermediate. J Am Chem Soc 2008, in press.
    • Hanes JW, Burns KE, Hilmey DG, Chatterjee A, Dorrestein PC, Begley TP: Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway leading to a chromophoric intermediate. J Am Chem Soc 2008, in press. Mechanistic characterization of the early steps involved in PLP biosynthesis.
  • 26
    • 41949139157 scopus 로고    scopus 로고
    • Hanes JW, Keresztes I, Begley TP: Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5′-phosphate. Angew Chem 2008, in press.
    • Hanes JW, Keresztes I, Begley TP: Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5′-phosphate. Angew Chem 2008, in press. A novel trapping strategy of an advanced intermediate involved in PLP biosynthesis.
  • 27
    • 22844442120 scopus 로고    scopus 로고
    • Crystal structure of the NAD biosynthetic enzyme quinolinate synthase
    • First reported structure of the NadA apoenzyme.
    • Sakuraba H., Tsuge H., Yoneda K., Katunuma N., and Ohshima T. Crystal structure of the NAD biosynthetic enzyme quinolinate synthase. J Biol Chem 280 (2005) 26645-26648. First reported structure of the NadA apoenzyme.
    • (2005) J Biol Chem , vol.280 , pp. 26645-26648
    • Sakuraba, H.1    Tsuge, H.2    Yoneda, K.3    Katunuma, N.4    Ohshima, T.5
  • 28
    • 19744378992 scopus 로고    scopus 로고
    • Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster
    • A combination of UV-visible, Mossbauer, and ESR spectroscopies demonstrated for the first time that anaerobically purified NadA from E. coli contained an Fe/S cluster.
    • Cicchillo R.M., Tu L., Stromberg J.A., Hoffart L.M., Krebs C., and Booker S.J. Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. J Am Chem Soc 127 (2005) 7310-7311. A combination of UV-visible, Mossbauer, and ESR spectroscopies demonstrated for the first time that anaerobically purified NadA from E. coli contained an Fe/S cluster.
    • (2005) J Am Chem Soc , vol.127 , pp. 7310-7311
    • Cicchillo, R.M.1    Tu, L.2    Stromberg, J.A.3    Hoffart, L.M.4    Krebs, C.5    Booker, S.J.6
  • 29
    • 19644363211 scopus 로고    scopus 로고
    • Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis
    • Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase in complex with 3-hydroxyanthranilate and nitric oxide clarifies the mechanism.
    • Zhang Y., Colabroy K.L., Begley T.P., and Ealick S.E. Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry 44 (2005) 7632-7643. Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase in complex with 3-hydroxyanthranilate and nitric oxide clarifies the mechanism.
    • (2005) Biochemistry , vol.44 , pp. 7632-7643
    • Zhang, Y.1    Colabroy, K.L.2    Begley, T.P.3    Ealick, S.E.4
  • 30
    • 12444320333 scopus 로고    scopus 로고
    • The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction
    • A model study on the ring opening of N,N-dimethylcarbamoylpyridinium with hydroxide and methoxide suggests that the pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction.
    • Colabroy K.L., and Begley T.P. The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction. J Am Chem Soc 127 (2005) 840-841. A model study on the ring opening of N,N-dimethylcarbamoylpyridinium with hydroxide and methoxide suggests that the pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction.
    • (2005) J Am Chem Soc , vol.127 , pp. 840-841
    • Colabroy, K.L.1    Begley, T.P.2
  • 31
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes
    • The first crystal structure of a radical SAM enzyme.
    • Layer G., Moser J., Heinz D.W., Jahn D., and Schubert W.-D. Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes. EMBO J 22 (2003) 6214-6224. The first crystal structure of a radical SAM enzyme.
    • (2003) EMBO J , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.-D.5
  • 32
    • 33744914624 scopus 로고    scopus 로고
    • The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN
    • EPR spectroscopic evidence for a relatively stable substrate-derived radical in the coproporphyrinogen III oxidase-catalyzed reaction.
    • Layer G., Pierik A.J., Trost M., Rigby S.E., Leech H.K., Grage K., Breckau D., Astner I., Jaensch L., Heathcote P., et al. The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN. J Biol Chem 281 (2006) 15727-15734. EPR spectroscopic evidence for a relatively stable substrate-derived radical in the coproporphyrinogen III oxidase-catalyzed reaction.
    • (2006) J Biol Chem , vol.281 , pp. 15727-15734
    • Layer, G.1    Pierik, A.J.2    Trost, M.3    Rigby, S.E.4    Leech, H.K.5    Grage, K.6    Breckau, D.7    Astner, I.8    Jaensch, L.9    Heathcote, P.10
  • 33
    • 33947529225 scopus 로고    scopus 로고
    • BluB cannibalizes flavin to form the lower ligand of vitamin B12
    • Structural studies on BluB clarify the mechanism of DMB formation from reduced FMN.
    • Taga M.E., Larsen N.A., Howard-Jones A.R., Walsh C.T., and Walker G.C. BluB cannibalizes flavin to form the lower ligand of vitamin B12. Nature 446 (2007) 449-453. Structural studies on BluB clarify the mechanism of DMB formation from reduced FMN.
    • (2007) Nature , vol.446 , pp. 449-453
    • Taga, M.E.1    Larsen, N.A.2    Howard-Jones, A.R.3    Walsh, C.T.4    Walker, G.C.5
  • 34
    • 33947527046 scopus 로고    scopus 로고
    • Biochemistry: molecular cannibalism
    • Ealick Steven E., and Begley Tadhg P. Biochemistry: molecular cannibalism. Nature 446 (2007) 387-388
    • (2007) Nature , vol.446 , pp. 387-388
    • Ealick Steven, E.1    Begley Tadhg, P.2


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