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Volumn 18, Issue 4, 2009, Pages 801-810

Relevance of weak flavin binding in human D-amino acid oxidase

Author keywords

Conformational change; Correlation of structure with spectra and other properties; circular dichroism; D serine; Enzymes; FAD binding; Flavoproteins; Fluorescence; Folding stability; Kinetics; mechanism enzymes; Neurotransmission; Protein structure folding; Regulation mechanism; Stability and mutagenesis

Indexed keywords

DEXTRO AMINO ACID OXIDASE; DEXTRO SERINE; FLAVOPROTEIN; HOLOENZYME; QUERCETIN;

EID: 63449109647     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.86     Document Type: Article
Times cited : (44)

References (18)
  • 2
    • 33746362592 scopus 로고    scopus 로고
    • D-serine signalling in the brain: Friend and foe
    • Martineau M, Baux G, Mothet JP (2006) D-serine signalling in the brain: friend and foe. Trends Neurosci 29: 481-491.
    • (2006) Trends Neurosci , vol.29 , pp. 481-491
    • Martineau, M.1    Baux, G.2    Mothet, J.P.3
  • 3
    • 0037108758 scopus 로고    scopus 로고
    • Chumakov I, Blumenfeld M, Guerassimenko O, Cavarec L, Palicio M, Abderrahim H, Bougueleret L, Barry C, Tanaka H, La Rosa P, Puech A, Tahri N, Cohen-Akenine A, Delabrosse S, Lissarrague S, Picard FP, Maurice K, Essionx L, Millasseau P, Grel P, Debailleul V, Simon AM, Caterina D, Dufaure I. Malekzadeh K. Belova M. Luan J.J, Bouillot M, Sambucy JL, Primas G, Saumier M, Boubkiri N, Martin-Saumier S, Nasroune M, Peixoto H, Delaye A, Pinchot V, Bastucci M, Guillou S, Chevillon M, Sainz-Fuertes K, Meguenni S, Aurich-Costa J, Cherif D, Gimalac A, Van Duijn C, Gauvreau D, Ouellette G, Fortier I, Raelson J, Sherbatich T, Riazanskaia N, Rogaev E, Raeymaekers P, Aerssens J, Konings F, Luyten W, Macciardi F, Sham PC, Straub RE, Weinberger DR, Cohen N, Cohen D (2002) Genetic and physiological data implicating the new human gene G72 and the gene for D-amino acid oxidase in schizophrenia. Proc Natl Acad Sci USA 99:13675-13680
    • Chumakov I, Blumenfeld M, Guerassimenko O, Cavarec L, Palicio M, Abderrahim H, Bougueleret L, Barry C, Tanaka H, La Rosa P, Puech A, Tahri N, Cohen-Akenine A, Delabrosse S, Lissarrague S, Picard FP, Maurice K, Essionx L, Millasseau P, Grel P, Debailleul V, Simon AM, Caterina D, Dufaure I. Malekzadeh K. Belova M. Luan J.J, Bouillot M, Sambucy JL, Primas G, Saumier M, Boubkiri N, Martin-Saumier S, Nasroune M, Peixoto H, Delaye A, Pinchot V, Bastucci M, Guillou S, Chevillon M, Sainz-Fuertes K, Meguenni S, Aurich-Costa J, Cherif D, Gimalac A, Van Duijn C, Gauvreau D, Ouellette G, Fortier I, Raelson J, Sherbatich T, Riazanskaia N, Rogaev E, Raeymaekers P, Aerssens J, Konings F, Luyten W, Macciardi F, Sham PC, Straub RE, Weinberger DR, Cohen N, Cohen D (2002) Genetic and physiological data implicating the new human gene G72 and the gene for D-amino acid oxidase in schizophrenia. Proc Natl Acad Sci USA 99:13675-13680.
  • 5
    • 33751519528 scopus 로고    scopus 로고
    • Crystal structure of human D-amino acid oxidase: Context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring
    • Kawazoe T, Tsuge H, Pilone MS, Fukui K (2006) Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci 15:2708-2717.
    • (2006) Protein Sci , vol.15 , pp. 2708-2717
    • Kawazoe, T.1    Tsuge, H.2    Pilone, M.S.3    Fukui, K.4
  • 6
    • 52049087606 scopus 로고    scopus 로고
    • PLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: Effect on schizophrenia susceptibility
    • Sacchi S, Bernasconi M, Martineau M, Mothet JP, Ruzzene M. Pilone MS, Pollegioni L, Molla G (2008) PLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: effect on schizophrenia susceptibility. J Biol Chem 283:22244-22256.
    • (2008) J Biol Chem , vol.283 , pp. 22244-22256
    • Sacchi, S.1    Bernasconi, M.2    Martineau, M.3    Mothet, J.P.4    Ruzzene, M.5    Pilone, M.S.6    Pollegioni, L.7    Molla, G.8
  • 7
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, Andrade-Navarro MA (2008) K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8:1-5.
    • (2008) BMC Struct Biol , vol.8 , pp. 1-5
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 8
    • 0030758374 scopus 로고    scopus 로고
    • Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis
    • Raibekas AA, Massey V (1997) Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis. J Biol Chem 272:22248- 22252.
    • (1997) J Biol Chem , vol.272 , pp. 22248-22252
    • Raibekas, A.A.1    Massey, V.2
  • 9
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein EA, Vedenkina NS, Ivkova MN (1973) Fluorescence and the location of tryptophan residues in protein molecules. Photochem Photobiol 18:263-279.
    • (1973) Photochem Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 10
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace CN (1990) Measuring and increasing protein stability. Trends Biotechnol 8:93-98.
    • (1990) Trends Biotechnol , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 13
    • 0014027814 scopus 로고
    • A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide
    • Massey V, Curti B (1966) A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide. J Biol Chem 241:3417-3423.
    • (1966) J Biol Chem , vol.241 , pp. 3417-3423
    • Massey, V.1    Curti, B.2
  • 14
    • 0030220402 scopus 로고    scopus 로고
    • On the holoenzyme reconstitution process in native and truncated Rhodotorula gracilis D-amino acid oxidase
    • Pollegioni L, Pilone MS (1996) On the holoenzyme reconstitution process in native and truncated Rhodotorula gracilis D-amino acid oxidase. Arch Biochem Biophys 332:58-62.
    • (1996) Arch Biochem Biophys , vol.332 , pp. 58-62
    • Pollegioni, L.1    Pilone, M.S.2
  • 15
    • 0029025347 scopus 로고
    • Extracellular concentration of endogenous free D-serine in the rat brain as revealed by in vivo microdialysis
    • Hashimoto A, Oka T, Nishikawa T (1995) Extracellular concentration of endogenous free D-serine in the rat brain as revealed by in vivo microdialysis. Neurosci 66: 635-643.
    • (1995) Neurosci , vol.66 , pp. 635-643
    • Hashimoto, A.1    Oka, T.2    Nishikawa, T.3
  • 16
    • 0019023389 scopus 로고
    • Riboflavin accumulation by rabbit brain slices, in vitro
    • Spector R (1980) Riboflavin accumulation by rabbit brain slices, in vitro J Neurosci 34:1768-1771.
    • (1980) J Neurosci , vol.34 , pp. 1768-1771
    • Spector, R.1
  • 17
    • 20744438190 scopus 로고    scopus 로고
    • Caldinelli L, lametti S, Barbiroli A, Bonomi F, Fessas D, Molla G, Pilone MS. Pollegioni L (2005) Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin, J Biol Chem 280:22572-22581.
    • Caldinelli L, lametti S, Barbiroli A, Bonomi F, Fessas D, Molla G, Pilone MS. Pollegioni L (2005) Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin, J Biol Chem 280:22572-22581.
  • 18
    • 20044363782 scopus 로고    scopus 로고
    • Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai Y, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR, Plaxco KW (2005) Protein folding: defining a standard set of experimental conditions and a preliminary kinetic data set of two-state proteins. Prot Sci 14:602-616.
    • Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai Y, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR, Plaxco KW (2005) Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Prot Sci 14:602-616.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.