메뉴 건너뛰기




Volumn 105, Issue 39, 2008, Pages 14849-14854

Discovery of posttranslational maturation by self-subunit swapping

Author keywords

Chaperone; Metalloenzyme; Modification; Sulfenic acid; Sulfinic acid

Indexed keywords

COBALT; CYSTEINE; HOLOENZYME; NITRILE HYDRATASE; APOENZYME; BACTERIAL PROTEIN; HYDROLYASE; METALLOPROTEIN; PROTEIN SUBUNIT;

EID: 54449092486     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0803428105     Document Type: Article
Times cited : (80)

References (43)
  • 1
    • 1542304722 scopus 로고    scopus 로고
    • Biosynthesis of metal sites
    • Kuchar J, Hausinger RP (2004) Biosynthesis of metal sites. Chem Rev 104:509-525.
    • (2004) Chem Rev , vol.104 , pp. 509-525
    • Kuchar, J.1    Hausinger, R.P.2
  • 2
    • 24344498616 scopus 로고    scopus 로고
    • Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy
    • Uchida T, Kitagawa T (2005) Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy. Acc Chem Res 38:662-670.
    • (2005) Acc Chem Res , vol.38 , pp. 662-670
    • Uchida, T.1    Kitagawa, T.2
  • 3
    • 0037047140 scopus 로고    scopus 로고
    • Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins
    • Lacourciere GM, Levine RL, Stadtman TC (2002) Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins. Proc Natl Acad Sci USA 99:9150-9153.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9150-9153
    • Lacourciere, G.M.1    Levine, R.L.2    Stadtman, T.C.3
  • 4
    • 0031879561 scopus 로고    scopus 로고
    • Metalloenzyme nitrile hydratase: Structure, regulation, and application to biotechnology
    • Kobayashi M, Shimizu S (1998) Metalloenzyme nitrile hydratase: Structure, regulation, and application to biotechnology. Nat Biotechnol 16:733-736.
    • (1998) Nat Biotechnol , vol.16 , pp. 733-736
    • Kobayashi, M.1    Shimizu, S.2
  • 5
    • 0000020934 scopus 로고
    • A new enzyme "nitrile hydratase" which degrades acetonitrile in combination with amidase
    • Asano Y, Tani Y, Yamada H (1980) A new enzyme "nitrile hydratase" which degrades acetonitrile in combination with amidase. Agric Biol Chem 44:2251-2252.
    • (1980) Agric Biol Chem , vol.44 , pp. 2251-2252
    • Asano, Y.1    Tani, Y.2    Yamada, H.3
  • 6
    • 0033152216 scopus 로고    scopus 로고
    • An enzyme controlled by light: The molecular mechanism of photoreactivity in nitrile hydratase
    • Endo I, Odaka M, Yohda M (1999) An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase. Trends Biotechnol 17:244-248.
    • (1999) Trends Biotechnol , vol.17 , pp. 244-248
    • Endo, I.1    Odaka, M.2    Yohda, M.3
  • 7
    • 0141954195 scopus 로고    scopus 로고
    • Protonation structures of Cys-sulfinic and Cys-sulfenic acids in the photosensitive nitrile hydratase revealed by Fourier transform infrared spectroscopy
    • Noguchi T, Nojiri M, Takei K, Odaka M, Kamiya N (2003) Protonation structures of Cys-sulfinic and Cys-sulfenic acids in the photosensitive nitrile hydratase revealed by Fourier transform infrared spectroscopy. Biochemistry 42:11642-11650.
    • (2003) Biochemistry , vol.42 , pp. 11642-11650
    • Noguchi, T.1    Nojiri, M.2    Takei, K.3    Odaka, M.4    Kamiya, N.5
  • 8
    • 0032064198 scopus 로고    scopus 로고
    • Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms
    • Nagashima S, et al. (1998) Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nat Struct Biol 5:347-351.
    • (1998) Nat Struct Biol , vol.5 , pp. 347-351
    • Nagashima, S.1
  • 9
    • 0031570299 scopus 로고    scopus 로고
    • Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold
    • Huang W, et al. (1997) Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure (London) 5:691-699.
    • (1997) Structure (London) , vol.5 , pp. 691-699
    • Huang, W.1
  • 10
    • 0029984895 scopus 로고    scopus 로고
    • A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product
    • Komeda H, Kobayashi M, Shimizu S (1996) A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product. J Biol Chem 271:15796-15802.
    • (1996) J Biol Chem , vol.271 , pp. 15796-15802
    • Komeda, H.1    Kobayashi, M.2    Shimizu, S.3
  • 11
    • 0030941934 scopus 로고    scopus 로고
    • A stereoselective cobalt-containing nitrile hydratase
    • Payne MS, et al. (1997) A stereoselective cobalt-containing nitrile hydratase. Biochemistry 36:5447-5454.
    • (1997) Biochemistry , vol.36 , pp. 5447-5454
    • Payne, M.S.1
  • 12
    • 1642561909 scopus 로고    scopus 로고
    • Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding
    • Miyanaga A, Fushinobu S, Ito K, Shoun H, Wakagi T (2004) Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding. Eur J Biochem 271:429-438.
    • (2004) Eur J Biochem , vol.271 , pp. 429-438
    • Miyanaga, A.1    Fushinobu, S.2    Ito, K.3    Shoun, H.4    Wakagi, T.5
  • 15
    • 0030700490 scopus 로고    scopus 로고
    • Identification of active sites in amidase: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes
    • Kobayashi M, Fujiwara Y, Goda M, Komeda H, Shimizu S (1997) Identification of active sites in amidase: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes. Proc Natl Acad Sci USA 94:11986-11991.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11986-11991
    • Kobayashi, M.1    Fujiwara, Y.2    Goda, M.3    Komeda, H.4    Shimizu, S.5
  • 16
    • 15744392913 scopus 로고    scopus 로고
    • Nitrile pathway involving acyl-CoA synthetase: Overall metabolic gene organization and purification and characterization of the enzyme
    • Hashimoto Y, et al. (2005) Nitrile pathway involving acyl-CoA synthetase: overall metabolic gene organization and purification and characterization of the enzyme. J Biol Chem 208:8660-8667.
    • (2005) J Biol Chem , vol.208 , pp. 8660-8667
    • Hashimoto, Y.1
  • 17
    • 45549093276 scopus 로고    scopus 로고
    • Discovery of amide (peptide) bond synthetic activity in Acyl-CoA synthetase
    • Abe T, et al. (2008) Discovery of amide (peptide) bond synthetic activity in Acyl-CoA synthetase. J Biol Chem 283:11312-11321.
    • (2008) J Biol Chem , vol.283 , pp. 11312-11321
    • Abe, T.1
  • 18
    • 0026480892 scopus 로고
    • Enzymatic synthesis of acrylamide: A success story not yet over
    • Kobayashi M, Nagasawa T, Yamada H (1992) Enzymatic synthesis of acrylamide: A success story not yet over. Trends Biotechnol 10:402-408.
    • (1992) Trends Biotechnol , vol.10 , pp. 402-408
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 19
    • 0042284991 scopus 로고    scopus 로고
    • Hydratases involved in nitrile conversion: Screening, characterization and application
    • Yamada H, Shimizu S, Kobayashi M (2001) Hydratases involved in nitrile conversion: Screening, characterization and application. Chem Res 1:152-161.
    • (2001) Chem Res , vol.1 , pp. 152-161
    • Yamada, H.1    Shimizu, S.2    Kobayashi, M.3
  • 20
    • 0032904843 scopus 로고    scopus 로고
    • Functional expression of nitrile hydratase in Escherichia coli: Requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine
    • Nojiri M, et al. (1999) Functional expression of nitrile hydratase in Escherichia coli: Requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine. J Biochem 125:696-704.
    • (1999) J Biochem , vol.125 , pp. 696-704
    • Nojiri, M.1
  • 21
    • 0025761763 scopus 로고
    • Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23
    • Nishiyama M, et al. (1991) Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23. J Bacteriol 173:2465-2472.
    • (1991) J Bacteriol , vol.173 , pp. 2465-2472
    • Nishiyama, M.1
  • 22
    • 0031450886 scopus 로고    scopus 로고
    • Over-production of stereoselective nitrile hydratase from Pseudomonas putida 5B in Escherichia coli: Activity requires a novel downstream protein
    • Wu S, Fallon R, Payne M (1997) Over-production of stereoselective nitrile hydratase from Pseudomonas putida 5B in Escherichia coli: Activity requires a novel downstream protein. Appl Microbiol Biotechnol 48:704-708.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 704-708
    • Wu, S.1    Fallon, R.2    Payne, M.3
  • 23
    • 0028519939 scopus 로고
    • Nitrile hydratase gene from Rhodococcus sp N-774 requirement for its downstream region for efficient expression
    • Hashimoto Y, Nishiyama M, Horinouchi S, Beppu T (1994) Nitrile hydratase gene from Rhodococcus sp N-774 requirement for its downstream region for efficient expression. Biosci Biotechnol Biochem 58:1859-1865.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1859-1865
    • Hashimoto, Y.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 24
    • 0142231423 scopus 로고    scopus 로고
    • Motif CXCC in nitrile hydratase activator is critical for NHase biogenesis in vivo
    • Lu J, et al. (2003) Motif CXCC in nitrile hydratase activator is critical for NHase biogenesis in vivo. FEBS Lett 553:391-396.
    • (2003) FEBS Lett , vol.553 , pp. 391-396
    • Lu, J.1
  • 25
    • 0029913827 scopus 로고    scopus 로고
    • Komeda H, Kobayashi M, Shimizu S (1996) Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1. Proc Natl Acad Sci USA 93:4267-4272.
    • Komeda H, Kobayashi M, Shimizu S (1996) Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1. Proc Natl Acad Sci USA 93:4267-4272.
  • 26
    • 0025934442 scopus 로고    scopus 로고
    • Kobayashi M, et al. (1991) Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1. Biochim Biophys Acta 1129:23-33.
    • Kobayashi M, et al. (1991) Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1. Biochim Biophys Acta 1129:23-33.
  • 28
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • Yamada H, Kobayashi M (1996) Nitrile hydratase and its application to industrial production of acrylamide. Biosci Biotech Biochem 60:1391-1400.
    • (1996) Biosci Biotech Biochem , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 29
    • 33746918762 scopus 로고    scopus 로고
    • Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K
    • Kataoka S, et al. (2006) Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K. FEBS Lett 580:4667-4672.
    • (2006) FEBS Lett , vol.580 , pp. 4667-4672
    • Kataoka, S.1
  • 30
    • 0033976042 scopus 로고    scopus 로고
    • Cobalt-substituted Fe-type nitrile hydratase of Rhodococcus sp N-771
    • Nojiri M, et al. (2000) Cobalt-substituted Fe-type nitrile hydratase of Rhodococcus sp N-771. FEBS Lett 465:173-177.
    • (2000) FEBS Lett , vol.465 , pp. 173-177
    • Nojiri, M.1
  • 31
    • 0000210346 scopus 로고    scopus 로고
    • Elder RC, Kennard GJ, Payne MD, Deutsch E (1978) Synthesis and characterization of bis(ethylenediamine)cobalt(III) complexes containing chelated thioether ligands. Crystal structures of, en)2Co(S(CH 3)CH2CH2NH2, Fe(CN)6] and, en)2Co(S(CH2C6H5)CH 2COO, SCN)2. Inorg Chem 17:1296-1303
    • 2. Inorg Chem 17:1296-1303.
  • 33
    • 0035941546 scopus 로고    scopus 로고
    • Why is there an "Inert" metal center in the active site of nitrile hydratase? Reactivity and ligand dissociation from a five-coordinate Co (III) nitrile hydratase model
    • Shearer J, Kung IY, Lovell S, Kaminsky W, Kovacs JA (2001) Why is there an "Inert" metal center in the active site of nitrile hydratase? Reactivity and ligand dissociation from a five-coordinate Co (III) nitrile hydratase model. J Am Chem Soc 123:463-468.
    • (2001) J Am Chem Soc , vol.123 , pp. 463-468
    • Shearer, J.1    Kung, I.Y.2    Lovell, S.3    Kaminsky, W.4    Kovacs, J.A.5
  • 34
    • 0034043871 scopus 로고    scopus 로고
    • Post-translational modification is essential for catalytic activity of nitrile hydratase
    • Murakami T, et al. (2000) Post-translational modification is essential for catalytic activity of nitrile hydratase. Protein Sci 9:1024-1030.
    • (2000) Protein Sci , vol.9 , pp. 1024-1030
    • Murakami, T.1
  • 35
    • 3543029884 scopus 로고    scopus 로고
    • Oxygen-induced maturation of SOD1: A key role for disulfide formation by the copper chaperone CCS
    • Furukawa Y, Torres AS, O'Halloran TV (2004) Oxygen-induced maturation of SOD1: A key role for disulfide formation by the copper chaperone CCS. EMBO J 23:2872-2881.
    • (2004) EMBO J , vol.23 , pp. 2872-2881
    • Furukawa, Y.1    Torres, A.S.2    O'Halloran, T.V.3
  • 36
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8:751-775.
    • (2001) Nat Struct Biol , vol.8 , pp. 751-775
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 37
    • 27944493626 scopus 로고    scopus 로고
    • The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo
    • Perlstein DL, et al. (2005) The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo. Biochemistry 44:15366-15377.
    • (2005) Biochemistry , vol.44 , pp. 15366-15377
    • Perlstein, D.L.1
  • 38
    • 2942711692 scopus 로고    scopus 로고
    • Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers
    • Sommerhalter M, et al. (2004) Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers. Biochemistry 43:7736-7742.
    • (2004) Biochemistry , vol.43 , pp. 7736-7742
    • Sommerhalter, M.1
  • 39
    • 35448984575 scopus 로고    scopus 로고
    • Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases
    • WangJ, Lohman GJS, Stubbe J (2007) Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases. Proc Natl Acad Sci USA 104:14324-14329.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14324-14329
    • Wang, J.1    Lohman, G.J.S.2    Stubbe, J.3
  • 40
    • 0027296628 scopus 로고
    • The. nifY product of Klebsiella pneumoniae is associated with apodinitrogenase and dissociates upon activation with the iron-molybdenum cofactor
    • Homer MJ, Paustian TD, Shah VK, Roberts GP (1993) The. nifY product of Klebsiella pneumoniae is associated with apodinitrogenase and dissociates upon activation with the iron-molybdenum cofactor. J Bacteriol 175:4907-4910.
    • (1993) J Bacteriol , vol.175 , pp. 4907-4910
    • Homer, M.J.1    Paustian, T.D.2    Shah, V.K.3    Roberts, G.P.4
  • 41
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 42
    • 34247644778 scopus 로고    scopus 로고
    • Topologies of a substrate protein bound to the chaperonin GroEL
    • Elad N, et al. (2007) Topologies of a substrate protein bound to the chaperonin GroEL. Mol Cell 26:415-426.
    • (2007) Mol Cell , vol.26 , pp. 415-426
    • Elad, N.1
  • 43
    • 23844552145 scopus 로고    scopus 로고
    • Molecular analysis of the nitrile catabolism operon of the thermophile Bacillus pallidus RAPc8
    • Cameron RA, Sayed M, Cowan DA (2005) Molecular analysis of the nitrile catabolism operon of the thermophile Bacillus pallidus RAPc8. Biochim Biophys Acta 1725:35-46.
    • (2005) Biochim Biophys Acta , vol.1725 , pp. 35-46
    • Cameron, R.A.1    Sayed, M.2    Cowan, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.