메뉴 건너뛰기




Volumn 86, Issue 6, 2010, Pages 1613-1619

Occurrence, characteristics, and applications of fructosyl amine oxidases (amadoriases)

Author keywords

Amadoriase; Applications; Characteristics; Fructosyl amine oxidase; Occurrence; Substrate specificity

Indexed keywords

AMADORI COMPOUND; AMADORIASE; CHRONIC DISEASE; CONSENSUS MOTIF; DIFFERENT SUBSTRATES; FRUCTOSYL AMINE OXIDASE; LYSINE RESIDUES; MAILLARD REACTION; NATURALLY OCCURRING; REDUCING SUGARS; SOLVED CRYSTAL STRUCTURES; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING SITES;

EID: 77952883142     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2523-5     Document Type: Short Survey
Times cited : (29)

References (55)
  • 1
    • 8144225715 scopus 로고    scopus 로고
    • Functional analysis of fructosyl-amino acid oxidases of Aspergillus oryzae
    • DOI 10.1128/AEM.70.10.5882-5890.2004
    • S Akazawa T Karino N Yoshida T Katsuragi Y Tani 2004 Functional analysis of fructosyl-amino acid oxidases of Aspergillus oryzae Appl Environ Microbiol 70 5882 5890 10.1128/AEM.70.10.5882-5890.2004 1:CAS:528:DC%2BD2cXosl2iur8%3D (Pubitemid 39471831)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.10 , pp. 5882-5890
    • Akazawa, S.-I.1    Karino, T.2    Yoshida, N.3    Katsuragi, T.4    Tani, Y.5
  • 2
    • 0034659178 scopus 로고    scopus 로고
    • Glycoxidation and lipoxidation in atherogenesis
    • DOI 10.1016/S0891-5849(00)00228-8, PII S0891584900002288
    • JW Baynes SR Thorpe 2000 Glycoxidation and lipoxidation in atherogenesis Free Rad Biol Med 28 1708 1716 10.1016/S0891-5849(00)00228-8 1:CAS:528:DC%2BD3cXls1Giu7k%3D (Pubitemid 30628657)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.12 , pp. 1708-1716
    • Baynes, J.W.1    Thorpe, S.R.2
  • 3
    • 55249095312 scopus 로고    scopus 로고
    • Crystal structure of the deglycating enzyme fructosamine oxidase (Amadoriase II)
    • 10.1074/jbc.M804885200 1:CAS:528:DC%2BD1cXhtFKhu7fF
    • F Collard J Zhang I Nemet KR Qanungo VM Monnier VC Yee 2008 Crystal structure of the deglycating enzyme fructosamine oxidase (Amadoriase II) J Biol Chem 283 27007 27016 10.1074/jbc.M804885200 1:CAS:528:DC%2BD1cXhtFKhu7fF
    • (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    Yee, V.C.6
  • 4
    • 0018787390 scopus 로고
    • Non-enzymatic glucosylation of rat albumin-studies in vitro and in vivo
    • 1:CAS:528:DyaE1MXlsFeisLs%3D
    • JF Day RW Thornburg SR Thorpe JW Baynes 1979 Non-enzymatic glucosylation of rat albumin-studies in vitro and in vivo J Biol Chem 254 9394 9400 1:CAS:528:DyaE1MXlsFeisLs%3D
    • (1979) J Biol Chem , vol.254 , pp. 9394-9400
    • Day, J.F.1    Thornburg, R.W.2    Thorpe, S.R.3    Baynes, J.W.4
  • 5
    • 60549116664 scopus 로고    scopus 로고
    • A single-use, disposable iridium-modified electrochemical biosensor for fructosyl valine for the glycoslated hemoglobin detection
    • 10.1016/j.snb.2008.09.045
    • L Fang W Li Y Zhou CC Liu 2009 A single-use, disposable iridium-modified electrochemical biosensor for fructosyl valine for the glycoslated hemoglobin detection Sens Actuator B Chem 137 235 238 10.1016/j.snb.2008.09.045
    • (2009) Sens Actuator B Chem , vol.137 , pp. 235-238
    • Fang, L.1    Li, W.2    Zhou, Y.3    Liu, C.C.4
  • 6
    • 19944414976 scopus 로고    scopus 로고
    • Cloning and expression of fructosyl-amine oxidase from marine yeast Pichia species N1-1
    • DOI 10.1007/s10126-004-0001-8
    • S Ferri S Miura A Sakaguchi F Ishimura W Tsugawa K Sode 2004 Cloning and expression of fructosyl-amine oxidase from marine yeast Pichia species N1-1 Mar Biotechnol 6 625 632 10.1007/s10126-004-0001-8 1:CAS:528:DC%2BD2MXjvF2ntLY%3D (Pubitemid 40747857)
    • (2004) Marine Biotechnology , vol.6 , Issue.6 , pp. 625-632
    • Ferri, S.1    Miura, S.2    Sakaguchi, A.3    Ishimura, F.4    Tsugawa, W.5    Sode, K.6
  • 7
    • 13844280841 scopus 로고    scopus 로고
    • Isolation and characterization of a fructosyl-amine oxidase from an Arthrobacter sp
    • DOI 10.1007/s10529-004-6312-z
    • S Ferri A Sakaguchi H Goto W Tsugawa K Sode 2005 Isolation and characterization of a fructosyl-amine oxidase from an Arthrobacter sp. Biotechnol Lett 27 27 32 10.1007/s10529-004-6312-z 1:CAS:528: DC%2BD2MXovFGqtA%3D%3D (Pubitemid 40252792)
    • (2005) Biotechnology Letters , vol.27 , Issue.1 , pp. 27-32
    • Ferri, S.1    Sakaguchi, A.2    Goto, H.3    Tsugawa, W.4    Sode, K.5
  • 9
    • 33847320650 scopus 로고    scopus 로고
    • Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum
    • 10.1007/s00253-006-0720-z 1:CAS:528:DC%2BD2sXitVKjs7Y%3D
    • M Fujiwara J Sumitani S Koga I Yoshioka T Kouzuma S Imamura T Kawaguchi M Arai 2007 Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum Appl Microbiol Biotechnol 74 813 819 10.1007/s00253-006-0720-z 1:CAS:528:DC%2BD2sXitVKjs7Y%3D
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 813-819
    • Fujiwara, M.1    Sumitani, J.2    Koga, S.3    Yoshioka, I.4    Kouzuma, T.5    Imamura, S.6    Kawaguchi, T.7    Arai, M.8
  • 10
    • 0023657734 scopus 로고
    • Molecular-cloning and sequence-analysis of cDNAs encoding porcine pidney d-amino-acid oxidase
    • 10.1021/bi00386a054 1:CAS:528:DyaL2sXkvFWju7g%3D
    • K Fukui F Watanabe T Shibata Y Miyake 1987 Molecular-cloning and sequence-analysis of cDNAs encoding porcine pidney d-amino-acid oxidase Biochemistry 26 3612 3618 10.1021/bi00386a054 1:CAS:528:DyaL2sXkvFWju7g%3D
    • (1987) Biochemistry , vol.26 , pp. 3612-3618
    • Fukui, K.1    Watanabe, F.2    Shibata, T.3    Miyake, Y.4
  • 11
    • 0020586544 scopus 로고
    • The principal site of nonenzymatic glycosylation of human serum albumin in vivo
    • 1:CAS:528:DyaL3sXktlCksrY%3D
    • RL Garlick JS Mazer 1983 The principal site of nonenzymatic glycosylation of human serum albumin in vivo J Biol Chem 258 6142 6146 1:CAS:528: DyaL3sXktlCksrY%3D
    • (1983) J Biol Chem , vol.258 , pp. 6142-6146
    • Garlick, R.L.1    Mazer, J.S.2
  • 12
    • 0028815495 scopus 로고
    • Novel degradation pathway of glycated amino-acids into free fructosamine by a Pseudomonas sp. soil strain extract
    • Gerhardinger C, Marion MS, Rovner A, Glomb M, Monnier VM (1995) Novel degradation pathway of glycated amino-acids into free fructosamine by a Pseudomonas sp. soil strain extract. J Biol Chem 270:218-224
    • (1995) J Biol Chem , vol.270 , pp. 218-224
    • Gerhardinger, C.1    Marion, M.S.2    Rovner, A.3    Glomb, M.4    Monnier, V.M.5
  • 13
    • 0027942845 scopus 로고
    • Isolation, purification, and characterization of an Amadori product binding-protein from a Pseudomonas sp. soil strain
    • 1:CAS:528:DyaK2cXmt1Cmtbs%3D
    • C Gerhardinger S Taneda MS Marion VM Monnier 1994 Isolation, purification, and characterization of an Amadori product binding-protein from a Pseudomonas sp. soil strain J Biol Chem 269 27297 27302 1:CAS:528: DyaK2cXmt1Cmtbs%3D
    • (1994) J Biol Chem , vol.269 , pp. 27297-27302
    • Gerhardinger, C.1    Taneda, S.2    Marion, M.S.3    Monnier, V.M.4
  • 14
    • 0029968456 scopus 로고    scopus 로고
    • Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin
    • MM Heath KC Rixon JJ Harding 1996 Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin BBA-Mol Basis Dis 1315 176 184
    • (1996) BBA-Mol Basis Dis , vol.1315 , pp. 176-184
    • Heath, M.M.1    Rixon, K.C.2    Harding, J.J.3
  • 15
    • 0042771552 scopus 로고    scopus 로고
    • Recombinant Agrobacterium AgaE-like protein with fructosyl amino acid oxidase activity
    • Hirokawa K, Kajiyama N (2002) Recombinant Agrobacterium AgaE-like protein with fructosyl amino acid oxidase activity. Biosci Biotechnol Biochem 66:2323-2329
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2323-2329
    • Hirokawa, K.1    Kajiyama, N.2
  • 16
    • 0041335497 scopus 로고    scopus 로고
    • Distribution and properties of novel deglycating enzymes for fructosyl peptide in fungi
    • DOI 10.1007/s00203-003-0584-x
    • K Hirokawa K Gomi M Bakke N Kajiyama 2003 Distribution and properties of novel deglycating enzymes for fructosyl peptide in fungi Arch Microbiol 180 227 231 10.1007/s00203-003-0584-x 1:CAS:528:DC%2BD3sXms1aju7Y%3D (Pubitemid 37102721)
    • (2003) Archives of Microbiology , vol.180 , Issue.3 , pp. 227-231
    • Hirokawa, K.1    Gomi, K.2    Bakke, M.3    Kajiyama, N.4
  • 17
    • 41049099149 scopus 로고    scopus 로고
    • Enhancement of thermostability of fungal deglycating enzymes by directed evolution
    • 10.1007/s00253-008-1363-z 1:CAS:528:DC%2BD1cXjsFGhtbo%3D
    • K Hirokawa A Ichiyanagi N Kajiyama 2008 Enhancement of thermostability of fungal deglycating enzymes by directed evolution Appl Microbiol Biotechnol 78 775 781 10.1007/s00253-008-1363-z 1:CAS:528:DC%2BD1cXjsFGhtbo%3D
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 775-781
    • Hirokawa, K.1    Ichiyanagi, A.2    Kajiyama, N.3
  • 18
    • 2442704308 scopus 로고    scopus 로고
    • Enzymes used for the determination of HbA(1C)
    • 10.1111/j.1574-6968.2004.tb09581.x 1:CAS:528:DC%2BD2cXktF2rs7c%3D
    • K Hirokawa K Nakamura N Kajiyama 2004 Enzymes used for the determination of HbA(1C) FEMS Microbiol Lett 235 157 162 10.1111/j.1574-6968.2004.tb09581.x 1:CAS:528:DC%2BD2cXktF2rs7c%3D
    • (2004) FEMS Microbiol Lett , vol.235 , pp. 157-162
    • Hirokawa, K.1    Nakamura, K.2    Kajiyama, N.3
  • 19
    • 18144415490 scopus 로고    scopus 로고
    • Should minimal blood glucose variability become the gold standard of glycemic control?
    • DOI 10.1016/j.jdiacomp.2004.10.001
    • IB Hirsch M Brownlee 2005 Should minimal blood glucose variability become the gold standard of glycemic control? J Diabetes Complicat 19 178 181 10.1016/j.jdiacomp.2004.10.001 (Pubitemid 40615551)
    • (2005) Journal of Diabetes and its Complications , vol.19 , Issue.3 , pp. 178-181
    • Hirsch, I.B.1    Brownlee, M.2
  • 20
    • 0000121228 scopus 로고
    • Purification and properties of fructosylamine oxidase from Aspergillus sp 1005
    • 1:CAS:528:DyaK3MXisVehsbc%3D
    • T Horiuchi T Kurokawa 1991 Purification and properties of fructosylamine oxidase from Aspergillus sp 1005 Agric Biol Chem 55 333 338 1:CAS:528: DyaK3MXisVehsbc%3D
    • (1991) Agric Biol Chem , vol.55 , pp. 333-338
    • Horiuchi, T.1    Kurokawa, T.2
  • 21
    • 0000908822 scopus 로고
    • Purification and properties of fructosyl-amino acid oxidase from Corynebacterium sp. 2-4-1
    • 1:CAS:528:DyaL1MXhvVyhsLg%3D
    • T Horiuchi T Kurokawa N Saito 1989 Purification and properties of fructosyl-amino acid oxidase from Corynebacterium sp. 2-4-1 Agric Biol Chem 53 103 110 1:CAS:528:DyaL1MXhvVyhsLg%3D
    • (1989) Agric Biol Chem , vol.53 , pp. 103-110
    • Horiuchi, T.1    Kurokawa, T.2    Saito, N.3
  • 24
    • 56549116514 scopus 로고    scopus 로고
    • Cumulative effect of amino acid substitution for the development of fructosyl valine-specific fructosyl amine oxidase
    • 10.1016/j.enzmictec.2008.09.001 1:CAS:528:DC%2BD1cXhsVCkt7fO
    • S Kim S Miura S Ferri W Tsugawa K Sode 2009 Cumulative effect of amino acid substitution for the development of fructosyl valine-specific fructosyl amine oxidase Enzyme Microb Technol 44 52 56 10.1016/j.enzmictec.2008.09.001 1:CAS:528:DC%2BD1cXhsVCkt7fO
    • (2009) Enzyme Microb Technol , vol.44 , pp. 52-56
    • Kim, S.1    Miura, S.2    Ferri, S.3    Tsugawa, W.4    Sode, K.5
  • 25
    • 0030853707 scopus 로고    scopus 로고
    • Candidate reference methods for hemoglobin A1c based on peptide mapping
    • 1:CAS:528:DyaK2sXmslGhtrk%3D
    • U Kobold J-O Jeppsson T Dulffer A Finke W Hoelzel K Miedema 1997 Candidate reference methods for hemoglobin A1c based on peptide mapping Clin Chem 43 1944 1951 1:CAS:528:DyaK2sXmslGhtrk%3D
    • (1997) Clin Chem , vol.43 , pp. 1944-1951
    • Kobold, U.1    Jeppsson, J.-O.2    Dulffer, T.3    Finke, A.4    Hoelzel, W.5    Miedema, K.6
  • 26
    • 0034633083 scopus 로고    scopus 로고
    • A review of Maillard reaction in food and implications to kinetic modelling
    • DOI 10.1016/S0924-2244(01)00022-X, PII S092422440100022X
    • SIFS Martins WMF Jongen MAJS van Boekel 2000 A review of Maillard reaction in food and implications to kinetic modelling Trends Food Sci Technol 11 364 373 10.1016/S0924-2244(01)00022-X 1:CAS:528:DC%2BD3MXktV2hu7s%3D (Pubitemid 32516039)
    • (2000) Trends in Food Science and Technology , vol.11 , Issue.9-10 , pp. 364-373
    • Martins, S.I.F.S.1    Jongen, W.M.F.2    Van Boekel, M.A.J.S.3
  • 27
    • 33750969391 scopus 로고    scopus 로고
    • Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis
    • DOI 10.1007/s10529-006-9173-9
    • S Miura S Ferri W Tsugawa S Kiin K Sode 2006 Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis Biotechnol Lett 28 1895 1900 10.1007/s10529-006-9173-9 1:CAS:528: DC%2BD28Xht1Sgu7rN (Pubitemid 44744797)
    • (2006) Biotechnology Letters , vol.28 , Issue.23 , pp. 1895-1900
    • Miura, S.1    Ferri, S.2    Tsugawa, W.3    Kim, S.4    Sode, K.5
  • 28
    • 41149102867 scopus 로고    scopus 로고
    • Development of fructosyl amine oxidase specific to fructosyl valine by site-directed mutagenesis
    • DOI 10.1093/protein/gzm047
    • S Miura S Ferri W Tsugawa S Kim K Sode 2008 Development of fructosyl amine oxidase specific to fructosyl valine by site-directed mutagenesis Protein Eng Des Sel 21 233 239 10.1093/protein/gzm047 1:CAS:528:DC%2BD1cXltleksbY%3D (Pubitemid 351431051)
    • (2008) Protein Engineering, Design and Selection , vol.21 , Issue.4 , pp. 233-239
    • Miura, S.1    Ferri, S.2    Tsugawa, W.3    Kim, S.4    Sode, K.5
  • 29
    • 0023681465 scopus 로고
    • Molecular-cloning and sequence-analysis of cDNA-encoding human-kidney d-amino-acid oxidase
    • 10.1016/0014-5793(88)80252-7 1:CAS:528:DyaL1MXktlCns74%3D
    • K Momoi K Fukui F Watanabe Y Miyake 1988 Molecular-cloning and sequence-analysis of cDNA-encoding human-kidney d-amino-acid oxidase FEBS Lett 238 180 184 10.1016/0014-5793(88)80252-7 1:CAS:528:DyaL1MXktlCns74%3D
    • (1988) FEBS Lett , vol.238 , pp. 180-184
    • Momoi, K.1    Fukui, K.2    Watanabe, F.3    Miyake, Y.4
  • 30
    • 33744956187 scopus 로고    scopus 로고
    • Prevention and repair of protein damage by the maillard reaction in vivo
    • DOI 10.1089/rej.2006.9.264
    • VM Monnier DR Sell 2006 Prevention and repair of protein damage by the Maillard reaction in vivo Rejuv Res 9 264 273 10.1089/rej.2006.9.264 1:CAS:528:DC%2BD28Xks1ajtLk%3D (Pubitemid 43856818)
    • (2006) Rejuvenation Research , vol.9 , Issue.2 , pp. 264-273
    • Monnier, V.M.1    Sell, D.R.2
  • 35
    • 0043175144 scopus 로고    scopus 로고
    • Development of highly-sensitive fructosyl-valine enzyme sensor employing recombinant fructosyl amine oxidase
    • 1:CAS:528:DC%2BD3sXksF2lsr8%3D
    • A Sakaguchi W Tsugawa S Ferri K Sode 2003 Development of highly-sensitive fructosyl-valine enzyme sensor employing recombinant fructosyl amine oxidase Electrochemistry 71 442 445 1:CAS:528:DC%2BD3sXksF2lsr8%3D
    • (2003) Electrochemistry , vol.71 , pp. 442-445
    • Sakaguchi, A.1    Tsugawa, W.2    Ferri, S.3    Sode, K.4
  • 36
    • 0029269211 scopus 로고
    • Purification and properties of fructosyl lysine oxidase from Fusarium oxysporum S-1F4
    • 10.1271/bbb.59.487 1:CAS:528:DyaK2MXkvVertbo%3D
    • Y Sakai N Yoshida A Isogai Y Tani N Kato 1995 Purification and properties of fructosyl lysine oxidase from Fusarium oxysporum S-1F4 Biosci Biotechnol Biochem 59 487 491 10.1271/bbb.59.487 1:CAS:528:DyaK2MXkvVertbo%3D
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 487-491
    • Sakai, Y.1    Yoshida, N.2    Isogai, A.3    Tani, Y.4    Kato, N.5
  • 37
    • 0037224714 scopus 로고    scopus 로고
    • Thermostabilization of bacterial fructosyl-amino acid oxidase by directed evolution
    • DOI 10.1128/AEM.69.1.139-145.2002
    • R Sakaue N Kajiyama 2003 Thermostabilization of bacterial fructosyl-amino acid oxidase by directed evolution Appl Environ Microbiol 69 139 145 10.1128/AEM.69.1.139-145.2002 1:CAS:528:DC%2BD3sXkvVagug%3D%3D (Pubitemid 36077468)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 139-145
    • Sakaue, R.1    Kajiyama, N.2
  • 38
    • 0036616988 scopus 로고    scopus 로고
    • Cloning and expression of fructosyl-amino acid oxidase gene from Corynebacterium sp. 2-4-1 in Escherichia coli
    • Sakaue R, Hiruma M, Kajiyama N, Koyama Y (2002) Cloning and expression of fructosyl-amino acid oxidase gene from Corynebacterium sp. 2-4-1 in Escherichia coli. Biosci Biotechnol Biochem 66:1256-1261
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1256-1261
    • Sakaue, R.1    Hiruma, M.2    Kajiyama, N.3    Koyama, Y.4
  • 40
    • 16944363204 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound deglycating enzyme (1-deoxyfructosyl alkyl amino acid oxidase, EC 1.5.3) from a Pseudomonas sp. soil strain
    • DOI 10.1074/jbc.271.51.32803
    • AK Saxena P Saxena VM Monnier 1996 Purification and characterization of a membrane-bound deglycating enzyme (1-deoxyfructosyl alkyl amino acid oxidase, EC 1.5.3) from a Pseudomonas sp. soil strain J Biol Chem 271 32803 32809 10.1074/jbc.271.51.32803 1:CAS:528:DyaK2sXntVCn (Pubitemid 27008709)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.51 , pp. 32803-32809
    • Saxena, A.K.1    Saxena, P.2    Monnier, V.M.3
  • 41
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human-serum albumin alters its conformation and function
    • 1:CAS:528:DyaL2cXhsFaksLg%3D
    • N Shaklai RL Garlick HF Bunn 1984 Nonenzymatic glycosylation of human-serum albumin alters its conformation and function J Biol Chem 259 3812 3817 1:CAS:528:DyaL2cXhsFaksLg%3D
    • (1984) J Biol Chem , vol.259 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 42
    • 0034807950 scopus 로고    scopus 로고
    • Screening and characterization of fructosyl-valine - Utilizing marine microorganisms
    • DOI 10.1007/s101260000065
    • K Sode F Ishimura W Tsugawa 2001 Screening and characterization of fructosyl-valine-utilizing marine microorganisms Mar Biotechnol 3 126 132 10.1007/s101260000065 1:CAS:528:DC%2BD3MXksVGnu7k%3D (Pubitemid 32925902)
    • (2001) Marine Biotechnology , vol.3 , Issue.2 , pp. 126-132
    • Sode, K.1    Ishimura, F.2    Tsugawa, W.3
  • 44
    • 0031031231 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of amadoriase isoenzymes (fructosyl amine-oxygen oxidoreductase EC 1.5.3) from Aspergillus sp
    • DOI 10.1074/jbc.272.6.3437
    • M Takahashi M Pischetsrieder VM Monnier 1997 Isolation, purification, and characterization of amadoriase isoenzymes (fructosyl amine-oxygen oxidoreductase EC 1.5.3) from Aspergillus sp. J Biol Chem 272 3437 3443 10.1074/jbc.272.6.3437 1:CAS:528:DyaK2sXhtFeltbg%3D (Pubitemid 27066842)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3437-3443
    • Takahashi, M.1    Pischetsrieder, M.2    Monnier, V.M.3
  • 45
    • 0030953790 scopus 로고    scopus 로고
    • Molecular cloning and expression of amadoriase isoenzyme (fructosyl amine:oxygen oxidoreductase, EC 1.5.3) from Aspergillus fumigatus
    • DOI 10.1074/jbc.272.19.12505
    • M Takahashi M Pischetsrieder VM Monnier 1997 Molecular cloning and expression of amadoriase isoenzyme (fructosyl amine: oxygen oxidoreductase, EC 1.5.3) from Aspergillus fumigatus J Biol Chem 272 12505 12507 10.1074/jbc.272.19.12505 1:CAS:528:DyaK2sXjtFyks7c%3D (Pubitemid 27203341)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.19 , pp. 12505-12507
    • Takahashi, M.1    Pischetsrieder, M.2    Monnier, V.M.3
  • 46
    • 0000560964 scopus 로고    scopus 로고
    • Development of an enzyme sensor utilizing a novel fructosyl amine oxidase from a marine yeast
    • 1:CAS:528:DC%2BD3cXnvVKjsLc%3D
    • W Tsugawa F Ishimura K Ogawa K Sode 2000 Development of an enzyme sensor utilizing a novel fructosyl amine oxidase from a marine yeast Electrochemistry 68 869 871 1:CAS:528:DC%2BD3cXnvVKjsLc%3D
    • (2000) Electrochemistry , vol.68 , pp. 869-871
    • Tsugawa, W.1    Ishimura, F.2    Ogawa, K.3    Sode, K.4
  • 47
    • 0035685275 scopus 로고    scopus 로고
    • Fructosyl amine sensing based on Prussian blue modified enzyme electrode
    • 1:CAS:528:DC%2BD3MXptVOhtbc%3D
    • W Tsugawa K Ogawa F Ishimura K Sode 2001 Fructosyl amine sensing based on Prussian blue modified enzyme electrode Electrochemistry 69 973 975 1:CAS:528:DC%2BD3MXptVOhtbc%3D
    • (2001) Electrochemistry , vol.69 , pp. 973-975
    • Tsugawa, W.1    Ogawa, K.2    Ishimura, F.3    Sode, K.4
  • 48
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding beta-alpha-beta-fold in proteins, using an amino-acid-sequence fingerprint
    • 10.1016/0022-2836(86)90409-2 1:CAS:528:DyaL28XhtVGmtLo%3D
    • RK Wierenga P Terpstra WGJ Hol 1986 Prediction of the occurrence of the ADP-binding beta-alpha-beta-fold in proteins, using an amino-acid-sequence fingerprint J Mol Biol 187 101 107 10.1016/0022-2836(86)90409-2 1:CAS:528:DyaL28XhtVGmtLo%3D
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 49
    • 0037006988 scopus 로고    scopus 로고
    • Alteration of substrate selectivity through mutation of two arginine residues in the binding site of amadoriase II from Aspergillus sp
    • DOI 10.1021/bi025539j
    • XL Wu SG Chen JM Petrash VM Monnier 2002 Alteration of substrate selectivity through mutation of two arginine residues in the binding site of amadoriase II from Aspergillus sp. Biochemistry 41 4453 4458 10.1021/bi025539j 1:CAS:528:DC%2BD38Xhslamur4%3D (Pubitemid 34259890)
    • (2002) Biochemistry , vol.41 , Issue.13 , pp. 4453-4458
    • Wu, X.1    Chen, S.G.2    Petrash, J.M.3    Monnier, V.M.4
  • 50
    • 0142058749 scopus 로고    scopus 로고
    • Enzymatic deglycation of proteins
    • DOI 10.1016/j.abb.2003.08.011
    • XL Wu VM Monnier 2003 Enzymatic deglycation of proteins Arch Biochem Biophys 419 16 24 10.1016/j.abb.2003.08.011 1:CAS:528:DC%2BD3sXotVCjur4%3D (Pubitemid 37272156)
    • (2003) Archives of Biochemistry and Biophysics , vol.419 , Issue.1 , pp. 16-24
    • Wu, X.1    Monnier, V.M.2
  • 51
    • 0034673106 scopus 로고    scopus 로고
    • Cloning of amadoriase i isoenzyme from Aspergillus sp.: Evidence of FAD covalently linked to Cys342
    • Wu XL, Takahashi M, Chen SG, Monnier VM (2000) Cloning of amadoriase I isoenzyme from Aspergillus sp.: evidence of FAD covalently linked to Cys342. Biochemistry 39:1515-1521
    • (2000) Biochemistry , vol.39 , pp. 1515-1521
    • Wu, X.L.1    Takahashi, M.2    Chen, S.G.3    Monnier, V.M.4
  • 53
    • 0030433513 scopus 로고    scopus 로고
    • Primary structures of fungal fructosyl amino acid oxidases and their application to the measurement of glycated proteins
    • 10.1111/j.1432-1033.1996.0499r.x 1:CAS:528:DyaK2sXlsFOnsg%3D%3D
    • N Yoshida Y Sakai A Isogai H Fukuya M Yagi Y Tani N Kato 1996 Primary structures of fungal fructosyl amino acid oxidases and their application to the measurement of glycated proteins Eur J Biochem 242 499 505 10.1111/j.1432-1033. 1996.0499r.x 1:CAS:528:DyaK2sXlsFOnsg%3D%3D
    • (1996) Eur J Biochem , vol.242 , pp. 499-505
    • Yoshida, N.1    Sakai, Y.2    Isogai, A.3    Fukuya, H.4    Yagi, M.5    Tani, Y.6    Kato, N.7
  • 54
    • 0028828672 scopus 로고
    • Distribution and properties of fructosyl amino-acid oxidase in fungi
    • 1:CAS:528:DyaK2MXpslCmtLY%3D
    • N Yoshida Y Sakai M Serata Y Tani N Kato 1995 Distribution and properties of fructosyl amino-acid oxidase in fungi Appl Environ Microbiol 61 4487 4489 1:CAS:528:DyaK2MXpslCmtLY%3D
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4487-4489
    • Yoshida, N.1    Sakai, Y.2    Serata, M.3    Tani, Y.4    Kato, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.