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Volumn 44, Issue 5, 2005, Pages 1659-1670

L-cysteine desulfidase: An [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; CATALYSIS; DECOMPOSITION; ELECTROPHORESIS; GELS; GENES; SULFUR;

EID: 13444311798     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0484769     Document Type: Article
Times cited : (40)

References (66)
  • 1
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., White, R. H., Cash, V. L., Jack, R. F., and Dean, D. R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 90, 2754-2758.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 2
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry 33, 4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 3
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: Their function and mechanisms
    • Mihara, H., and Esaki, N. (2002) Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Biotechnol. 60, 12-23.
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 4
    • 0022311120 scopus 로고
    • D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization
    • Nagasawa, T., Ishii, T., Kumagai, H., and Yamada, H. (1985) D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Eur. J. Biochem. 153, 541-551.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 541-551
    • Nagasawa, T.1    Ishii, T.2    Kumagai, H.3    Yamada, H.4
  • 5
    • 0032923527 scopus 로고    scopus 로고
    • Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. Analyses using cystine analogues and recombinant C-DES
    • Lang, T., and Kessler, D. (1999) Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. Analyses using cystine analogues and recombinant C-DES. J. Biol. Chem. 274, 189-195.
    • (1999) J. Biol. Chem. , vol.274 , pp. 189-195
    • Lang, T.1    Kessler, D.2
  • 6
    • 0030978491 scopus 로고    scopus 로고
    • A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin
    • Leibrecht, I., and Kessler, D. (1997) A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin. J. Biol. Chem. 272, 10442-10447.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10442-10447
    • Leibrecht, I.1    Kessler, D.2
  • 7
    • 0031616701 scopus 로고    scopus 로고
    • Mechanisms of cysteine S-conjugate β-lyases
    • Cooper, A. J. (1998) Mechanisms of cysteine S-conjugate β-lyases. Adv. Enzymol. Relat. Areas Mol. Biol. 72, 199-238.
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.72 , pp. 199-238
    • Cooper, A.J.1
  • 8
    • 0020490539 scopus 로고
    • Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme
    • Esaki, N., Nakamura, T., Tanaka, H., and Soda, K. (1982) Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. J. Biol. Chem. 257, 4386-4391.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4386-4391
    • Esaki, N.1    Nakamura, T.2    Tanaka, H.3    Soda, K.4
  • 9
    • 0022259475 scopus 로고
    • Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii
    • Chocat, P., Esaki, N., Tanizawa, K., Nakamura, K., Tanaka, H., and Soda, K. (1985) Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii. J. Bacteriol. 163, 669-676.
    • (1985) J. Bacteriol. , vol.163 , pp. 669-676
    • Chocat, P.1    Esaki, N.2    Tanizawa, K.3    Nakamura, K.4    Tanaka, H.5    Soda, K.6
  • 10
    • 0034673177 scopus 로고    scopus 로고
    • Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase
    • Fujii, T., Maeda, M., Mihara, H., Kurihara, T., Esaki, N., and Hata, Y. (2000) Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry 39, 1263-1273.
    • (2000) Biochemistry , vol.39 , pp. 1263-1273
    • Fujii, T.1    Maeda, M.2    Mihara, H.3    Kurihara, T.4    Esaki, N.5    Hata, Y.6
  • 12
    • 0028315145 scopus 로고
    • Enzymology of cysteine S-conjugate β-lyases
    • Cooper, A. J. (1994) Enzymology of cysteine S-conjugate β-lyases. Adv. Pharmacol. 27, 71-113.
    • (1994) Adv. Pharmacol. , vol.27 , pp. 71-113
    • Cooper, A.J.1
  • 13
    • 0030957220 scopus 로고    scopus 로고
    • Mode of action of cystathionine β-lyase
    • Clausen, T., Laber, B., and Messerschmidt, A. (1997) Mode of action of cystathionine β-lyase. Biol. Chem. 378, 321-326.
    • (1997) Biol. Chem. , vol.378 , pp. 321-326
    • Clausen, T.1    Laber, B.2    Messerschmidt, A.3
  • 14
    • 0345258439 scopus 로고    scopus 로고
    • The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii
    • White, R. H. (2003) The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii. Biochim. Biophys. Acta 1624, 46-53.
    • (2003) Biochim. Biophys. Acta , vol.1624 , pp. 46-53
    • White, R.H.1
  • 15
    • 0001531847 scopus 로고    scopus 로고
    • Iron-Sulfur Proteins with nonredox functions
    • Flint, D. H., and Allen, R. M. (1996) Iron-Sulfur Proteins with nonredox functions. Chem. Rev. 96, 2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 16
    • 0027934012 scopus 로고
    • Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: Correlation of the cluster type with enzymatic activity
    • Hofmeister, A. E., Albracht, S. P., and Buckel, W. (1994) Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: correlation of the cluster type with enzymatic activity. FEBS Lett. 351, 416-418.
    • (1994) FEBS Lett. , vol.351 , pp. 416-418
    • Hofmeister, A.E.1    Albracht, S.P.2    Buckel, W.3
  • 18
    • 0022478456 scopus 로고
    • Effect of sulfur-containing compounds on growth of Methanosarcina barkeri in defined medium
    • Mazumder, T. K., Nishio, N., Fukuzaki, S., and Nagai, S. (1986) Effect of sulfur-containing compounds on growth of Methanosarcina barkeri in defined medium. Appl. Environ. Microbiol. 52, 617-622.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 617-622
    • Mazumder, T.K.1    Nishio, N.2    Fukuzaki, S.3    Nagai, S.4
  • 19
    • 0000095103 scopus 로고
    • Characterization of the enzymatic conversion of sulfoacetaldehyde and L-cysteine into coenzyme M (2-mercaptoethanesulfonic acid)
    • White, R. H. (1988) Characterization of the enzymatic conversion of sulfoacetaldehyde and L-cysteine into coenzyme M (2-mercaptoethanesulfonic acid). Biochemistry 27, 7458-7462.
    • (1988) Biochemistry , vol.27 , pp. 7458-7462
    • White, R.H.1
  • 20
    • 0020400917 scopus 로고
    • Preparation of 3-mercaptolactic acid and S-aminoethylmercaptolactic acid
    • Costa, M., Pensa, B., Iavarone, C., and Cavallini, D. (1982) Preparation of 3-mercaptolactic acid and S-aminoethylmercaptolactic acid. Prepr. Biochem. 12, 417-427.
    • (1982) Prepr. Biochem. , vol.12 , pp. 417-427
    • Costa, M.1    Pensa, B.2    Iavarone, C.3    Cavallini, D.4
  • 21
    • 0032731169 scopus 로고    scopus 로고
    • Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities
    • Mukhopadhyay, B., Johnson, E. F., and Wolfe, R. S. (1999) Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities. Appl. Environ. Microbiol. 65, 5059-5065.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5059-5065
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 22
    • 0018337819 scopus 로고
    • Fluorometric determination of pyridoxal phosphate in enzymes
    • Adams, E. (1979) Fluorometric determination of pyridoxal phosphate in enzymes. Methods Enzymol. 62, 407-410.
    • (1979) Methods Enzymol. , vol.62 , pp. 407-410
    • Adams, E.1
  • 23
    • 0037134521 scopus 로고    scopus 로고
    • Identification of coenzyme M biosynthetic phosphosulfolactate synthase: A new family of sulfonate biosynthesizing enzymes
    • Graham, D. E., Xu, H., and White, R. H. (2002) Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate biosynthesizing enzymes. J. Biol. Chem. 277, 13421-13429.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13421-13429
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 24
    • 0033893841 scopus 로고    scopus 로고
    • Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M
    • Graupner, M., Xu, H., and White, R. H. (2000) Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 182, 4862-4867.
    • (2000) J. Bacteriol. , vol.182 , pp. 4862-4867
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 25
    • 0037837811 scopus 로고    scopus 로고
    • The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase
    • Li, H., Xu, H., Graham, D. E., and White, R. H. (2003) The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278, 11100-11106.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11100-11106
    • Li, H.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 26
    • 0026637901 scopus 로고
    • Purification and characterization of O-acetylserine (thiol) lyase from spinach chloroplasts
    • Droux, M., Martin, J., Sajus, P., and Douce, R. (1992) Purification and characterization of O-acetylserine (thiol) lyase from spinach chloroplasts. Arch. Biochem. Biophys. 295, 379-390.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 379-390
    • Droux, M.1    Martin, J.2    Sajus, P.3    Douce, R.4
  • 27
    • 0019594741 scopus 로고
    • A method for the measurement of the abundance of sulfur-34 in protein-bound cysteine and methionine
    • White, R. H. (1981) A method for the measurement of the abundance of sulfur-34 in protein-bound cysteine and methionine. Anal. Biochem. 114, 349-354.
    • (1981) Anal. Biochem. , vol.114 , pp. 349-354
    • White, R.H.1
  • 28
    • 0031572227 scopus 로고    scopus 로고
    • Biosynthesis of the peptide bond in the coenzyme N-(7-mercaptoheptanoyl)- L-threonine phosphate
    • Solow, B., and White, R. H. (1997) Biosynthesis of the peptide bond in the coenzyme N-(7-mercaptoheptanoyl)-L-threonine phosphate. Arch. Biochem. Biophys. 345, 299-304.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 299-304
    • Solow, B.1    White, R.H.2
  • 29
    • 0034099657 scopus 로고    scopus 로고
    • Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea
    • Graupner, M., Xu, H., and White, R. H. (2000) Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182, 3688-3692.
    • (2000) J. Bacteriol. , vol.182 , pp. 3688-3692
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 30
    • 33947443367 scopus 로고
    • Determination of iron with o-phenanthroline
    • Fortune, W. B., and Mellon, M. G. (1938) Determination of iron with o-phenanthroline. Ind. Eng. Chem. Anal. Ed. 10, 61-64.
    • (1938) Ind. Eng. Chem. Anal. Ed. , vol.10 , pp. 61-64
    • Fortune, W.B.1    Mellon, M.G.2
  • 32
    • 0025874803 scopus 로고
    • Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus
    • Grabowski, R., and Buckel, W. (1991) Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus. Eur. J. Biochem. 199, 89-94.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 89-94
    • Grabowski, R.1    Buckel, W.2
  • 33
    • 0021112560 scopus 로고
    • Optical and EPR characterization of different species of active and inactive aconitase
    • Emptage, M. H., Dreyers, J. L., Kennedy, M. C., and Beinert, H. (1983) Optical and EPR characterization of different species of active and inactive aconitase. J. Biol. Chem. 258, 11106-11111.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11106-11111
    • Emptage, M.H.1    Dreyers, J.L.2    Kennedy, M.C.3    Beinert, H.4
  • 34
    • 0027375778 scopus 로고
    • The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated
    • Flint, D. H., Smyk-Randall, E., Tuminello, J. F., Draczynska-Lusiak, B., and Brown, O. R. (1993) The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated. J. Biol. Chem. 268, 25547-25552.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25547-25552
    • Flint, D.H.1    Smyk-Randall, E.2    Tuminello, J.F.3    Draczynska-Lusiak, B.4    Brown, O.R.5
  • 35
    • 0019966186 scopus 로고
    • Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mossbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II
    • Moura, J. J., Moura, I., Kent, T. A., Lipscomb, J. D., Huynh, B. H., LeGall, J., Xavier, A. V., and Munck, E. (1982) Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mossbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II. J. Biol. Chem. 257, 6259-6267.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6259-6267
    • Moura, J.J.1    Moura, I.2    Kent, T.A.3    Lipscomb, J.D.4    Huynh, B.H.5    LeGall, J.6    Xavier, A.V.7    Munck, E.8
  • 36
    • 0021893322 scopus 로고
    • Mossbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters
    • Kent, T. A., Emptage, M. H., Merkle, H., Kennedy, M. C., Beinert, H., and Munck, E. (1985) Mossbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters. J. Biol. Chem. 260, 6871-6881.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6871-6881
    • Kent, T.A.1    Emptage, M.H.2    Merkle, H.3    Kennedy, M.C.4    Beinert, H.5    Munck, E.6
  • 38
    • 0030021889 scopus 로고    scopus 로고
    • A serine cysteine ligand mutation in the high potential iron-sulfur protein from Chromatium vinosum provides insight into the electronic structure of the [4Fe-4S] cluster
    • Babini, E., Bertini, I., Borsari, M., Capozzi, F., Eltis, L. D., and Lunchinat, C. (1996) A serine cysteine ligand mutation in the high potential iron-sulfur protein from Chromatium vinosum provides insight into the electronic structure of the [4Fe-4S] cluster. J. Am. Chem. Soc. 118, 75-80.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 75-80
    • Babini, E.1    Bertini, I.2    Borsari, M.3    Capozzi, F.4    Eltis, L.D.5    Lunchinat, C.6
  • 40
    • 0032490087 scopus 로고    scopus 로고
    • The rubredoxin from Clostridium pasteurianum: Mutation of the iron cysteinyl ligands to serine. Crystal and molecular structures of oxidized and dithionine-treated forms of the Cys42Ser mutant
    • Xiao, Z., Lavery, M. J., Ayhan, M., Scrofani, D. B., Wilce, M. C. J., Guss, J. M., Tregloan, P. A., Geroge, G. N., and Wedd, A. G. (1998) The rubredoxin from Clostridium pasteurianum: Mutation of the iron cysteinyl ligands to serine. Crystal and molecular structures of oxidized and dithionine-treated forms of the Cys42Ser mutant. J. Am. Chem. Soc. 120, 4135-4150.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4135-4150
    • Xiao, Z.1    Lavery, M.J.2    Ayhan, M.3    Scrofani, D.B.4    Wilce, M.C.J.5    Guss, J.M.6    Tregloan, P.A.7    Geroge, G.N.8    Wedd, A.G.9
  • 43
    • 0029908553 scopus 로고    scopus 로고
    • Cysteine ligand swapping on a deletable loop of the [2Fe-2S] ferredoxin from Clostridium pasteurianum
    • Golinelli, M. P., Akin, L. A., Crouse, B. R., Johnson, M. K., and Meyer, J. (1996) Cysteine ligand swapping on a deletable loop of the [2Fe-2S] ferredoxin from Clostridium pasteurianum. Biochemistry 35, 8995-9002.
    • (1996) Biochemistry , vol.35 , pp. 8995-9002
    • Golinelli, M.P.1    Akin, L.A.2    Crouse, B.R.3    Johnson, M.K.4    Meyer, J.5
  • 44
    • 0027181333 scopus 로고
    • L-serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups
    • Hofmeister, A. E., Grabowski, R., Linder, D., and Buckel, W. (1993) L-serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups. Eur. J. Biochem. 215, 341-349.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 341-349
    • Hofmeister, A.E.1    Grabowski, R.2    Linder, D.3    Buckel, W.4
  • 45
    • 0030838035 scopus 로고    scopus 로고
    • Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: Relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli
    • Hofmeister, A. E., Textor, S., and Buckel, W. (1997) Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli. J. Bacteriol. 179, 4937-4941.
    • (1997) J. Bacteriol. , vol.179 , pp. 4937-4941
    • Hofmeister, A.E.1    Textor, S.2    Buckel, W.3
  • 46
    • 0027247728 scopus 로고
    • Bacterial L-serine dehydratases: A new family of enzymes containing iron-sulfur clusters
    • Grabowski, R., Hofmeister, A. E., and Buckel, W. (1993) Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters. Trends Biochem. Sci. 18, 297-300.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 297-300
    • Grabowski, R.1    Hofmeister, A.E.2    Buckel, W.3
  • 47
    • 85021622696 scopus 로고
    • Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions
    • Gerlt, J. A., Kozarich, J. W., Kenyon, G. L., and Gassman, P. G. (1991) Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions. J. Am. Chem. Soc. 113, 9667-9669.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9667-9669
    • Gerlt, J.A.1    Kozarich, J.W.2    Kenyon, G.L.3    Gassman, P.G.4
  • 48
    • 1842800737 scopus 로고
    • Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions
    • Gerlt, J. A., and Gassman, P. G. (1992) Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions. J. Am. Chem. Soc. 114, 5928-5934.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5928-5934
    • Gerlt, J.A.1    Gassman, P.G.2
  • 49
    • 0037174377 scopus 로고    scopus 로고
    • An anchoring role for FeS clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formatelyase activating enzyme
    • Walsby, C. J., Ortillo, D., Broderick, W. E., Broderick, J. B., and Hoffman, B. M. (2002) An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formatelyase activating enzyme. J. Am. Chem. Soc. 124, 11270-11271.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 50
    • 0141620318 scopus 로고    scopus 로고
    • Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase
    • Chen, D., Walsby, C., Hoffman, B. M., and Frey, P. A. (2003) Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase. J. Am. Chem. Soc. 125, 11788-11789.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11788-11789
    • Chen, D.1    Walsby, C.2    Hoffman, B.M.3    Frey, P.A.4
  • 51
    • 0016791954 scopus 로고
    • Reaction mechanism and structure of the active site of proline racemase
    • Rudnick, G., and Abeles, R. H. (1975) Reaction mechanism and structure of the active site of proline racemase. Biochemistry 14, 4515-4522.
    • (1975) Biochemistry , vol.14 , pp. 4515-4522
    • Rudnick, G.1    Abeles, R.H.2
  • 52
    • 0027155359 scopus 로고
    • Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase
    • Tanner, M. E., Gallo, K. A., and Knowles, J. R. (1993) Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase. Biochemistry 32, 3998-4006.
    • (1993) Biochemistry , vol.32 , pp. 3998-4006
    • Tanner, M.E.1    Gallo, K.A.2    Knowles, J.R.3
  • 53
    • 0026655552 scopus 로고
    • Properties of aspartate racemase, a pyridoxal 5′-phosphate- independent amino acid racemase
    • Yamauchi, T., Choi, S. Y., Okada, H., Yohda, M., Kumagai, H., Esaki, N., and Soda, K. (1992) Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase. J. Biol. Chem. 267, 18361-18364.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18361-18364
    • Yamauchi, T.1    Choi, S.Y.2    Okada, H.3    Yohda, M.4    Kumagai, H.5    Esaki, N.6    Soda, K.7
  • 54
    • 0032564314 scopus 로고    scopus 로고
    • Structural symmetry: The three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase
    • Cirilli, M., Zheng, R., Scapin, G., and Blanchard, J. S. (1998) Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry 37, 16452-16458.
    • (1998) Biochemistry , vol.37 , pp. 16452-16458
    • Cirilli, M.1    Zheng, R.2    Scapin, G.3    Blanchard, J.S.4
  • 56
    • 0001673360 scopus 로고
    • Attack of zwitterionic ammonium thiolates on a distorted anilide as a model for the acylation of papain by amides. A simple demonstration of a bell-shaped pH/rate profile
    • Keillor, J. W., and Brown, R. S. (1992) Attack of zwitterionic ammonium thiolates on a distorted anilide as a model for the acylation of papain by amides. A simple demonstration of a bell-shaped pH/rate profile. J. Am. Chem. Soc. 114, 7983-7989.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7983-7989
    • Keillor, J.W.1    Brown, R.S.2
  • 57
    • 0026738940 scopus 로고
    • Mutational analysis of active site residues in pig heart aconitase
    • Zheng, L., Kennedy, M. C., Beinert, H., and Zalkin, H. (1992) Mutational analysis of active site residues in pig heart aconitase. J. Biol. Chem. 267, 7895-7903.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7895-7903
    • Zheng, L.1    Kennedy, M.C.2    Beinert, H.3    Zalkin, H.4
  • 58
    • 0026587755 scopus 로고
    • Crystal structures of aconitase with isocitrate and nitroisocitrate bound
    • Lauble, H., Kennedy, M. C., Beinert, H., and Stout, C. D. (1992) Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Biochemistry 31, 2735-2748.
    • (1992) Biochemistry , vol.31 , pp. 2735-2748
    • Lauble, H.1    Kennedy, M.C.2    Beinert, H.3    Stout, C.D.4
  • 59
    • 0033436322 scopus 로고    scopus 로고
    • The mechanism of aconitase: 1.8 A resolution crystal structure of the S642A:citrate complex
    • Lloyd, S. J., Lauble, H., Prasad, G. S., and Stout, C. D. (1999) The mechanism of aconitase: 1.8 A resolution crystal structure of the S642A:citrate complex. Protein Sci. 8, 2655-2662.
    • (1999) Protein Sci. , vol.8 , pp. 2655-2662
    • Lloyd, S.J.1    Lauble, H.2    Prasad, G.S.3    Stout, C.D.4
  • 60
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • Frazzon, J., and Dean, D. R. (2003) Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7, 166-173.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 61
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 277, 28380-28383.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 63
    • 2442473182 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein
    • Dos Santos, P. C., Smith, A. D., Frazzon, J., Cash, V. L., Johnson, M. K., and Dean, D. R. (2004) Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein. J. Biol. Chem. 279, 19705-19711.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19705-19711
    • Dos Santos, P.C.1    Smith, A.D.2    Frazzon, J.3    Cash, V.L.4    Johnson, M.K.5    Dean, D.R.6
  • 64
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar, J. N., Krebs, C., Frazzon, J., Huynh, B. H., Dean, D. R., and Johnson, M. K. (2000) IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 39, 7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 66
    • 0030056113 scopus 로고    scopus 로고
    • Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases a and B and β-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis
    • Flint, D. H., Tuminello, J. F., and Miller, T. J. (1996) Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and β-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis. J. Biol. Chem. 271, 16053-16067.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16053-16067
    • Flint, D.H.1    Tuminello, J.F.2    Miller, T.J.3


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