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Volumn 49, Issue 17, 2010, Pages 3631-3639

Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase

Author keywords

[No Author keywords available]

Indexed keywords

APPARENT KINETICS; BINDING CAVITY; BULK SOLVENTS; OXYGEN ACTIVATIONS; OXYGEN REACTIVITY; OXYGEN REDUCTION; PROTON-RELAY SYSTEMS; REACTION INTERMEDIATE; SARCOSINE; SARCOSINE OXIDASE; SIDE CHAINS; STRUCTURAL CHARACTERIZATION; STRUCTURAL WATER; WILD TYPES;

EID: 77951698123     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100160j     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes Trends Biochem. Sci. 31, 276-283
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 2
    • 70549103613 scopus 로고    scopus 로고
    • The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: Structural biology and biomolecular simulation
    • Baron, R., McCammon, J. A., and Mattevi, A. (2009) The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: Structural biology and biomolecular simulation Curr. Opin. Struct. Biol. 19, 672-679
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 672-679
    • Baron, R.1    McCammon, J.A.2    Mattevi, A.3
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
    • 0034254540 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase. 1. Flavin reactivity and active site binding determinants
    • Wagner, M. A., Trickey, P., Chen, Z., Mathews, F. S., and Jorns, M. S. (2000) Monomeric sarcosine oxidase. 1. Flavin reactivity and active site binding determinants Biochemistry 39, 8813-8824
    • (2000) Biochemistry , vol.39 , pp. 8813-8824
    • Wagner, M.A.1    Trickey, P.2    Chen, Z.3    Mathews, F.S.4    Jorns, M.S.5
  • 7
    • 0034254672 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase. 2. Kinetic studies with sarcosine, alternate substrates and substrate analogs
    • Wagner, M. A. and Jorns, M. S. (2000) Monomeric sarcosine oxidase. 2. Kinetic studies with sarcosine, alternate substrates and substrate analogs Biochemistry 39, 8825-8829
    • (2000) Biochemistry , vol.39 , pp. 8825-8829
    • Wagner, M.A.1    Jorns, M.S.2
  • 8
    • 0001390566 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Structure of a covalently-flavinylated secondary amine oxidizing enzyme
    • 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
    • (1999) Structure , vol.7 , pp. 331-345
    • Trickey, P.1    Wagner, M.A.2    Jorns, M.S.3    Mathews, F.S.4
  • 9
    • 0035814809 scopus 로고    scopus 로고
    • Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli
    • Khanna, P. and Jorns, M. S. (2001) Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli Biochemistry 40, 1441-1450
    • (2001) Biochemistry , vol.40 , pp. 1441-1450
    • Khanna, P.1    Jorns, M.S.2
  • 10
    • 44349132154 scopus 로고    scopus 로고
    • The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity
    • Ilari, A., Bonamore, A., Franceschini, S., Fiorillo, A., Boffi, A., and Colotti, G. (2008) The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity Proteins 71, 2065-2075
    • (2008) Proteins , vol.71 , pp. 2065-2075
    • Ilari, A.1    Bonamore, A.2    Franceschini, S.3    Fiorillo, A.4    Boffi, A.5    Colotti, G.6
  • 11
    • 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 Å resolution
    • 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
    • (2007) Structure , vol.15 , 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
  • 12
    • 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
    • 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
    • (2000) Biochem. J. , vol.345 , 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
  • 13
    • 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
  • 14
    • 33746128802 scopus 로고    scopus 로고
    • Heterotetrameric sarcosine oxidase: Structure of a diflavin metalloenzyme at 1.85 Å resolution
    • Chen, Z., Hassan-Abdallah, A., Zhao, G., Jorns, M. S., and Mathews, F. S. (2006) Heterotetrameric sarcosine oxidase: Structure of a diflavin metalloenzyme at 1.85 Å resolution J. Mol. Biol. 360, 1000-1018
    • (2006) J. Mol. Biol. , vol.360 , pp. 1000-1018
    • Chen, Z.1    Hassan-Abdallah, A.2    Zhao, G.3    Jorns, M.S.4    Mathews, F.S.5
  • 15
    • 0029143934 scopus 로고
    • Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism
    • Chlumky, L. J., Zhang, L., and Jorns, M. S. (1995) Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism J. Biol. Chem. 270, 18252-18259
    • (1995) J. Biol. Chem. , vol.270 , pp. 18252-18259
    • Chlumky, L.J.1    Zhang, L.2    Jorns, M.S.3
  • 16
    • 0029913243 scopus 로고    scopus 로고
    • Sarcosine oxidase contains a novel covalently bound FMN
    • Willie, A., Edmondson, D. E., and Jorns, M. S. (1996) Sarcosine oxidase contains a novel covalently bound FMN Biochemistry 35, 5292-5299
    • (1996) Biochemistry , vol.35 , pp. 5292-5299
    • Willie, A.1    Edmondson, D.E.2    Jorns, M.S.3
  • 17
    • 0022974540 scopus 로고
    • Bacterial sarcosine oxidase: Comparison of two multisubunit enzymes containing both covalent and noncovalent flavin
    • Kvalnes-Krick, K. and Jorns, M. S. (1986) Bacterial sarcosine oxidase: Comparison of two multisubunit enzymes containing both covalent and noncovalent flavin Biochemistry 25, 6061-6069
    • (1986) Biochemistry , vol.25 , pp. 6061-6069
    • Kvalnes-Krick, K.1    Jorns, M.S.2
  • 18
    • 0030996664 scopus 로고    scopus 로고
    • Cloning and functional expression of a mammalian gene for a peroxisomal sarcosine oxidase
    • Reuber, B. E., Karl, C., Reimann, S. A., Mihalik, S. J., and Dodt, G. (1997) Cloning and functional expression of a mammalian gene for a peroxisomal sarcosine oxidase J. Biol. Chem. 272, 6766-6776
    • (1997) J. Biol. Chem. , vol.272 , pp. 6766-6776
    • Reuber, B.E.1    Karl, C.2    Reimann, S.A.3    Mihalik, S.J.4    Dodt, G.5
  • 19
    • 33750969391 scopus 로고    scopus 로고
    • Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis
    • Miura, S., Ferri, S., Tsugawa, W., Kiin, S., and Sode, K. (2006) Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis Biotechnol. Lett. 28, 1895-1900
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1895-1900
    • Miura, S.1    Ferri, S.2    Tsugawa, W.3    Kiin, S.4    Sode, K.5
  • 20
    • 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
  • 21
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • Binda, C., Li, M., Hubalek, F., Restelli, N., Edmondson, D. E., and Mattevi, A. (2003) Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures Proc. Natl. Acad. Sci. U.S.A. 100, 9750-9755
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.E.5    Mattevi, A.6
  • 22
    • 34548519907 scopus 로고    scopus 로고
    • A 30 angstrom long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • 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
    • (1999) Structure , vol.7 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 23
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase A at 2.2 Å resolution: The control of opening the entry for substrates/inhibitors
    • Son, S., Ma, J., Kondou, Y., Yoshimura, M., Yamashita, E., and Tsukihara, T. (2008) Structure of human monoamine oxidase A at 2.2 Å resolution: The control of opening the entry for substrates/inhibitors Proc. Natl. Acad. Sci. U.S.A. 105, 5739-5744
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5739-5744
    • Son, S.1    Ma, J.2    Kondou, Y.3    Yoshimura, M.4    Yamashita, E.5    Tsukihara, T.6
  • 24
    • 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
    • (2000) EMBO J. , vol.19 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    MacHeroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 26
    • 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
    • (1994) J. Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelyhood method
    • Murshudov, G., Vagin, A., and Dodson, E. (1997) Refinement of macromolecular structures by the maximum likelyhood method Acta Crystallogr. D53, 240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.2    Dodson, E.3
  • 31
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Application of the free r value
    • Kleywegt, G. J. and Brünger, A. T. (1996) Checking your imagination: Application of the free r value Structure 4, 897-904
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 32
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.-S. and Brünger, A. T. (1994) Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures J. Mol. Biol. 243, 100-115
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 40149093398 scopus 로고    scopus 로고
    • Arg49 is a bifunctional residue important in catalysis and biosynthesis of monomeric sarcosine oxidase: A context-sensitive model for the electrostatic impact of arginine to lysine mutations
    • Hassan-Abdallah, A., Zhao, G., Chen, Z., Mathews, F. S., and Jorns, M. S. (2008) Arg49 is a bifunctional residue important in catalysis and biosynthesis of monomeric sarcosine oxidase: A context-sensitive model for the electrostatic impact of arginine to lysine mutations Biochemistry 47, 2913-2922
    • (2008) Biochemistry , vol.47 , pp. 2913-2922
    • Hassan-Abdallah, A.1    Zhao, G.2    Chen, Z.3    Mathews, F.S.4    Jorns, M.S.5
  • 35
    • 33646576258 scopus 로고    scopus 로고
    • Spectral and kinetic characterization of the Michaelis charge transfer complex in monomeric sarcosine oxidase
    • 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
    • (2006) Biochemistry , vol.45 , pp. 5985-5992
    • Zhao, G.1    Jorns, M.S.2
  • 36
    • 0037031276 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Role of histidine 269 in catalysis
    • Zhao, G., Song, H., Chen, Z., Mathews, F. S., and Jorns, M. S. (2002) Monomeric sarcosine oxidase: Role of histidine 269 in catalysis Biochemistry 41, 9751-9764
    • (2002) Biochemistry , vol.41 , pp. 9751-9764
    • Zhao, G.1    Song, H.2    Chen, Z.3    Mathews, F.S.4    Jorns, M.S.5
  • 37
    • 29344450649 scopus 로고    scopus 로고
    • Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase
    • Zhao, G. and Jorns, M. S. (2005) Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase Biochemistry 44, 16866-16874
    • (2005) Biochemistry , vol.44 , pp. 16866-16874
    • Zhao, G.1    Jorns, M.S.2
  • 38
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia, C. (1976) The nature of the accessible and buried surfaces in proteins J. Mol. Biol. 105, 1-14
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-14
    • Chothia, C.1
  • 39
    • 0037046142 scopus 로고    scopus 로고
    • Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry
    • 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
    • (2002) Biochemistry , vol.41 , 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
  • 40
    • 34547122265 scopus 로고    scopus 로고
    • Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor
    • Heuts, D. P. H. M., van Hellemond, E. W., Janssen, D. B., and Fraaije, M. W. (2007) Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor J. Biol. Chem. 282, 20283-20291
    • (2007) J. Biol. Chem. , vol.282 , pp. 20283-20291
    • Heuts, D.P.H.M.1    Van Hellemond, E.W.2    Janssen, D.B.3    Fraaije, M.W.4
  • 41
    • 70350045277 scopus 로고    scopus 로고
    • Disruption of the proton relay network in the class 2 dihydroorotate dehydrogenase from Escherichia coli
    • Kow, R. L., Whicher, J. R., McDonald, C. A., Palfey, B. A., and Fagan, R. L. (2009) Disruption of the proton relay network in the class 2 dihydroorotate dehydrogenase from Escherichia coli Biochemistry 48, 9801-9809
    • (2009) Biochemistry , vol.48 , pp. 9801-9809
    • Kow, R.L.1    Whicher, J.R.2    McDonald, C.A.3    Palfey, B.A.4    Fagan, R.L.5


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