메뉴 건너뛰기




Volumn 50, Issue 22, 2011, Pages 4949-4962

Pleiotropic impact of a single lysine mutation on biosynthesis of and catalysis by N-methyltryptophan oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; APOPROTEINS; CHARGE-TRANSFER BANDS; COMPLEX DISSOCIATES; COVALENTLY BOUND; IN-VIVO; LYSINE MUTATION; MUTANT ENZYMES; N-METHYLTRYPTOPHAN OXIDASE; OXYGEN ACTIVATIONS; OXYGEN REDUCTION; REDOX-ACTIVE; TURNOVER RATE; WILD TYPES;

EID: 79958065906     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200349m     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 14344257032 scopus 로고    scopus 로고
    • pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
    • DOI 10.1021/bi047716h
    • Ralph, E. C. and Fitzpatrick, P. F. (2005) pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase Biochemistry 44, 3074-3081 (Pubitemid 40293682)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 3074-3081
    • Ralph, E.C.1    Fitzpatrick, P.F.2
  • 2
    • 0035814817 scopus 로고    scopus 로고
    • N-methyltryptophan oxidase from Escherichia coli: Reaction kinetics with N-methyl amino acid and carbinolamine substrates
    • DOI 10.1021/bi002442t
    • Khanna, P. and Jorns, M. S. (2001) N-Methyltryptophan oxidase from Escherichia coli: Reaction kinetics with N-methyl amino acid and carbinolamine substrates Biochemistry 40, 1451-1459 (Pubitemid 32142907)
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1451-1459
    • Khanna, P.1    Jorns, M.S.2
  • 3
    • 0035814809 scopus 로고    scopus 로고
    • Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli
    • DOI 10.1021/bi0024411
    • Khanna, P. and Jorns, M. S. (2001) Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli Biochemistry 40, 1441-1450 (Pubitemid 32142906)
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1441-1450
    • Khanna, P.1    Jorns, M.S.2
  • 4
    • 0033609040 scopus 로고    scopus 로고
    • Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and N-methyltryptophan oxidase
    • Wagner, M. A., Khanna, P., and Jorns, M. S. (1999) Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and N-methyltryptophan oxidase Biochemistry 38, 5588-5595
    • (1999) Biochemistry , vol.38 , pp. 5588-5595
    • Wagner, M.A.1    Khanna, P.2    Jorns, M.S.3
  • 6
    • 0001390566 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Structure of a covalently flavinylated amine oxidizing enzyme
    • DOI 10.1016/S0969-2126(99)80043-4
    • Trickey, P., Wagner, M. A., Jorns, M. S., and Mathews, F. S. (1999) Monomeric sarcosine oxidase: Structure of a covalently-flavinylated secondary amine oxidizing enzyme Structure 7, 331-345 (Pubitemid 29159692)
    • (1999) Structure , vol.7 , Issue.3 , pp. 331-345
    • Trickey, P.1    Wagner, M.A.2    Jorns, M.S.3    Mathews, F.S.4
  • 7
    • 34547663087 scopus 로고    scopus 로고
    • NikD, an Unusual Amino Acid Oxidase Essential for Nikkomycin Biosynthesis: Structures of Closed and Open Forms at 1.15 and 1.90 A Resolution
    • DOI 10.1016/j.str.2007.06.010, PII S0969212607002407
    • Carrell, C. J., Bruckner, R. C., Venci, D., Zhao, G., Jorns, M. S., and Mathews, F. S. (2007) NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: Structures of closed and open forms at 1.15 and 1.90 Å resolution Structure 15, 928-941 (Pubitemid 47212748)
    • (2007) Structure , vol.15 , Issue.8 , pp. 928-941
    • Carrell, C.J.1    Bruckner, R.C.2    Venci, D.3    Zhao, G.4    Jorns, M.S.5    Mathews, F.S.6
  • 8
    • 0034141356 scopus 로고    scopus 로고
    • L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases
    • DOI 10.1042/0264-6021:3450487
    • Dodt, G., Kim, D. G., Reimann, S. A., Reuber, B. E., McCabe, K., Gould, S. J., and Mihalik, S. J. (2000) l -Pipecolic acid oxidase, a human enzyme essential for the degradation of l -pipecolic acid, is most similar to the monomeric sarcosine oxidases Biochem. J. 345, 487-494 (Pubitemid 30099077)
    • (2000) Biochemical Journal , vol.345 , Issue.3 , pp. 487-494
    • Dodt, G.1    Kim, D.G.2    Reimann, S.A.3    Reuber, B.E.4    McCabe, K.5    Gould, S.J.6    Mihalik, S.J.7
  • 9
    • 55249095312 scopus 로고    scopus 로고
    • Crystal structure of the deglycating enzyme fructosamine oxidase (amadoriase II)
    • Collard, F., Zhang, J., Nemet, I., Qanungo, K. R., and Monnier, V. M. (2008) Crystal structure of the deglycating enzyme fructosamine oxidase (amadoriase II) J. Biol. Chem. 283, 27007-27016
    • (2008) J. Biol. Chem. , vol.283 , pp. 27007-27016
    • Collard, F.1    Zhang, J.2    Nemet, I.3    Qanungo, K.R.4    Monnier, V.M.5
  • 10
    • 85063492372 scopus 로고
    • Role of the covalent and noncovalent flavins in sarcosine oxidase
    • In (Ed.) pp, CRC Press Inc., Boca Raton, FL
    • Kvalnes-Krick, K. and Jorns, M. S. (1991) Role of the covalent and noncovalent flavins in sarcosine oxidase. In Chemistry and Biochemistry of Flavoenzymes (Muller, F., Ed.) pp 425-435, CRC Press Inc., Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 425-435
    • Kvalnes-Krick, K.1    Jorns, M.S.2    Muller, F.3
  • 11
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins J. Biol. Chem. 269, 22459-22462 (Pubitemid 24273342)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.36 , pp. 22459-22462
    • Massey, V.1
  • 12
    • 34447638717 scopus 로고    scopus 로고
    • How do enzymes activate oxygen without inactivating themselves?
    • Klinman, J. P. (2007) How do enzymes activate oxygen without inactivating themselves? Acc. Chem. Res. 40, 325-333
    • (2007) Acc. Chem. Res. , vol.40 , pp. 325-333
    • Klinman, J.P.1
  • 13
    • 50849101652 scopus 로고    scopus 로고
    • Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis
    • Zhao, G., Bruckner, R. C., and Jorns, M. S. (2008) Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis Biochemistry 47, 9124-9135
    • (2008) Biochemistry , vol.47 , pp. 9124-9135
    • Zhao, G.1    Bruckner, R.C.2    Jorns, M.S.3
  • 14
    • 77951698123 scopus 로고    scopus 로고
    • Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase
    • Jorns, M. S., Chen, Z., and Mathews, F. S. (2010) Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase Biochemistry 49, 3631-3639
    • (2010) Biochemistry , vol.49 , pp. 3631-3639
    • Jorns, M.S.1    Chen, Z.2    Mathews, F.S.3
  • 15
    • 70350063829 scopus 로고    scopus 로고
    • Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by nikD, an unusual amino acid oxidase
    • Kommoju, P. R., Bruckner, R. C., Ferreira, P., Carrell, C. J., Mathews, F. S., and Jorns, M. S. (2009) Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by nikD, an unusual amino acid oxidase Biochemistry 48, 9542-9555
    • (2009) Biochemistry , vol.48 , pp. 9542-9555
    • Kommoju, P.R.1    Bruckner, R.C.2    Ferreira, P.3    Carrell, C.J.4    Mathews, F.S.5    Jorns, M.S.6
  • 16
    • 12344251747 scopus 로고    scopus 로고
    • 466 of choline oxidase
    • DOI 10.1021/bi048056j
    • Ghanem, M. and Gadda, G. (2005) On the catalytic role of the conserved active site residue His466 of choline oxidase Biochemistry 44, 893-904 (Pubitemid 40129649)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 893-904
    • Ghanem, M.1    Gadda, G.2
  • 17
    • 33745713811 scopus 로고    scopus 로고
    • On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase
    • Gadda, G., Fan, F., and Hoang, J. V. (2006) On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase Arch. Biochem. Biophys. 451, 182-187
    • (2006) Arch. Biochem. Biophys. , vol.451 , pp. 182-187
    • Gadda, G.1    Fan, F.2    Hoang, J.V.3
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77, 51-59 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 19
    • 0016207266 scopus 로고
    • Identification and properties of new flavins in electron-transferring flavoprotein from Peptostreptococcus elsdenii and pig liver glycolic acid oxidase
    • Mayhew, S. G., Whitfield, C. D., Ghisla, S., and Jorns, M. S. (1974) Identification and properties of new flavins in electron-transferring flavoprotein from Peptostreptococcus elsdenii and pig liver glycolic acid oxidase Eur. J. Biochem. 44, 579-591
    • (1974) Eur. J. Biochem. , vol.44 , pp. 579-591
    • Mayhew, S.G.1    Whitfield, C.D.2    Ghisla, S.3    Jorns, M.S.4
  • 20
    • 17844393348 scopus 로고    scopus 로고
    • Biosynthesis of covalently bound flavin: Isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein
    • DOI 10.1021/bi047271x
    • Hassan-Abdallah, A., Bruckner, R. C., Zhao, G., and Jorns, M. S. (2005) Biosynthesis of covalently bound flavin: Isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein Biochemistry 44, 6452-6462 (Pubitemid 40593796)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6452-6462
    • Hassan-Abdallah, A.1    Bruckner, R.C.2    Zhao, G.3    Jorns, M.S.4
  • 21
    • 66349094817 scopus 로고    scopus 로고
    • Spectral and kinetic characterization of intermediates in the aromatization reaction catalyzed by nikD, an unusual amino acid oxidase
    • Bruckner, R. C. and Jorns, M. S. (2009) Spectral and kinetic characterization of intermediates in the aromatization reaction catalyzed by nikD, an unusual amino acid oxidase Biochemistry 48, 4455-4465
    • (2009) Biochemistry , vol.48 , pp. 4455-4465
    • Bruckner, R.C.1    Jorns, M.S.2
  • 22
    • 33646576258 scopus 로고    scopus 로고
    • Spectral and kinetic characterization of the Michaelis charge transfer complex in monomeric sarcosine oxidase
    • DOI 10.1021/bi0600852
    • Zhao, G. and Jorns, M. S. (2006) Spectral and kinetic characterization of the Michaelis charge transfer complex in monomeric sarcosine oxidase Biochemistry 45, 5985-5992 (Pubitemid 43727090)
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 5985-5992
    • Zhao, G.1    Jorns, M.S.2
  • 23
    • 0023664644 scopus 로고
    • D -Aspartate oxidase from beef kidney
    • Negri, A., Massey, V., and Williams, C. H. J. (1987) d -Aspartate oxidase from beef kidney J. Biol. Chem. 262, 10026-10034
    • (1987) J. Biol. Chem. , vol.262 , pp. 10026-10034
    • Negri, A.1    Massey, V.2    Williams, C.H.J.3
  • 25
    • 24744466510 scopus 로고    scopus 로고
    • The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity
    • DOI 10.1074/jbc.M414018200
    • Marshall, K. R., Gong, M., Wodke, L., Lamb, J. H., Jones, D. J. L., Farmer, P. B., Scrutton, N. S., and Munro, A. W. (2005) The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity J. Biol. Chem. 280, 30735-30740 (Pubitemid 41291802)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30735-30740
    • Marshall, K.R.1    Gong, M.2    Wodke, L.3    Lamb, J.H.4    Jones, D.J.L.5    Farmer, P.B.6    Scrutton, N.S.7    Munro, A.W.8
  • 26
    • 0029935833 scopus 로고    scopus 로고
    • Reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine
    • DOI 10.1074/jbc.271.23.13401
    • Huang, L. X., Scrutton, N. S., and Hille, R. (1996) Reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine J. Biol. Chem. 271, 13401-13406 (Pubitemid 26185380)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13401-13406
    • Huang, L.1    Scrutton, N.S.2    Hille, R.3
  • 27
    • 0242380212 scopus 로고    scopus 로고
    • A mechanism for substrate-induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase
    • DOI 10.1016/j.bmcl.2003.07.032
    • Lu, X. L., Nikolic, D., Mitchell, D. J., van Breemen, R. B., Mersfelder, J. A., Hille, R., and Silverman, R. B. (2003) A mechanism for substrate-induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase Bioorg. Med. Chem. Lett. 13, 4129-4132 (Pubitemid 37338461)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.22 , pp. 4129-4132
    • Lu, X.1    Nikolic, D.2    Mitchell, D.J.3    Van Breemen, R.B.4    Mersfelder, J.A.5    Hille, R.6    Silverman, R.B.7
  • 28
    • 38349156041 scopus 로고    scopus 로고
    • Structural analysis of the catalytic mechanism and stereo selectivity in Streptomyces coelicolor alditol oxidase
    • Forneris, F., Heuts, D. P. H. M., Delvecchio, M., Rovida, S., Fraaije, M. W., and Mattevi, A. (2008) Structural analysis of the catalytic mechanism and stereo selectivity in Streptomyces coelicolor alditol oxidase Biochemistry 47, 978-985
    • (2008) Biochemistry , vol.47 , pp. 978-985
    • Forneris, F.1    Heuts, D.P.H.M.2    Delvecchio, M.3    Rovida, S.4    Fraaije, M.W.5    Mattevi, A.6
  • 29
    • 79551718687 scopus 로고    scopus 로고
    • Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex
    • Baron, R., Binda, C., Tortorici, M., McCammon, J. A., and Mattevi, A. (2011) Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex Structure 19, 212-220
    • (2011) Structure , vol.19 , pp. 212-220
    • Baron, R.1    Binda, C.2    Tortorici, M.3    McCammon, J.A.4    Mattevi, A.5
  • 31
    • 0037031242 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Evidence for an ionizable group in the E·S complex
    • DOI 10.1021/bi020285n
    • Zhao, G. and Jorns, M. S. (2002) Monomeric sarcosine oxidase: Evidence for an ionizable group in the ES complex Biochemistry 41, 9747-9750 (Pubitemid 34839722)
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 9747-9750
    • Zhao, G.1    Jorns, M.S.2
  • 32
    • 0037046142 scopus 로고    scopus 로고
    • Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry
    • DOI 10.1021/bi025519h
    • Basran, J., Bhanji, N., Basran, A., Nietlispach, D., Mistry, S., Meskys, R., and Scrutton, N. S. (2002) Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry Biochemistry 41, 4733-4743 (Pubitemid 34275674)
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4733-4743
    • Basran, J.1    Bhanji, N.2    Basran, A.3    Nietlispach, D.4    Mistry, S.5    Meskys, R.6    Scrutton, N.S.7
  • 35
    • 34548519907 scopus 로고    scopus 로고
    • A 30 A long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • DOI 10.1016/S0969-2126(99)80037-9
    • Binda, C., Coda, A., Angelini, R., Federico, R., Ascenzi, P., and Mattevi, A. (1999) A 30 angstrom long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase Structure 7, 265-276 (Pubitemid 29159686)
    • (1999) Structure , vol.7 , Issue.3 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 37
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • Pawelek, P. D., Cheah, J., Coulombe, R., Macheroux, P., Ghisla, S., and Vrielink, A. (2000) The structure of l -amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site EMBO J. 19, 4204-4215 (Pubitemid 30623731)
    • (2000) EMBO Journal , vol.19 , Issue.16 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 39
    • 50849089044 scopus 로고    scopus 로고
    • Studies on the role of lysine-296 in human mitochondrial monoamine oxidase B catalysis
    • Kacar, B. and Edmondson, D. E. (2006) Studies on the role of lysine-296 in human mitochondrial monoamine oxidase B catalysis FASEB J. 20, A478-A479
    • (2006) FASEB J. , vol.20
    • Kacar, B.1    Edmondson, D.E.2
  • 40
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • DOI 10.1038/nature04021, PII N04021
    • Lee, M. G., Wynder, C., Cooch, N., and Shiekhattar, R. (2005) An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation Nature 437, 432-435 (Pubitemid 41613507)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 42
    • 77953538248 scopus 로고    scopus 로고
    • A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase
    • Pozzi, M. H. and Fitzpatrick, P. F. (2010) A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase Arch. Biochem. Biophys. 498, 83-88
    • (2010) Arch. Biochem. Biophys. , vol.498 , pp. 83-88
    • Pozzi, M.H.1    Fitzpatrick, P.F.2
  • 43
    • 79951950697 scopus 로고    scopus 로고
    • The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation
    • Fiorillo, A., Federico, R., Polticelli, F., Boffi, A., Mazzei, F., Di Fusco, M., Ilari, A., and Tavladoraki, P. (2011) The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation FEBS J. 278, 809-821
    • (2011) FEBS J. , vol.278 , pp. 809-821
    • Fiorillo, A.1    Federico, R.2    Polticelli, F.3    Boffi, A.4    Mazzei, F.5    Di Fusco, M.6    Ilari, A.7    Tavladoraki, P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.