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Volumn 78, Issue 3, 2008, Pages 455-463

Discovery and characterization of a putrescine oxidase from Rhodococcus erythropolis NCIMB 11540

Author keywords

Activity screening; Amine; Flavin; Putrescine oxidase

Indexed keywords

ACTIVITY SCREENING; ADENINE DINUCLEOTIDES; FLAVOPROTEIN; PUTRESCINE OXIDASE; SUBSTRATE BINDING;

EID: 39149120591     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1310-4     Document Type: Article
Times cited : (38)

References (31)
  • 1
    • 0035202117 scopus 로고    scopus 로고
    • Molecular characterization of monoamine oxidases a and B
    • Abell CW, Kwan SW (2001) Molecular characterization of monoamine oxidases A and B. Prog Nucleic Acid Res Mol Biol 65:129-156
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.65 , pp. 129-156
    • Abell, C.W.1    Kwan, S.W.2
  • 2
    • 0037008967 scopus 로고    scopus 로고
    • Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution
    • Alexeeva M, Enright A, Dawson MJ, Mahmoudian M, Turner N (2002) Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution. Angew Chem Int Ed 41:3177-3180
    • (2002) Angew Chem Int Ed , vol.41 , pp. 3177-3180
    • Alexeeva, M.1    Enright, A.2    Dawson, M.J.3    Mahmoudian, M.4    Turner, N.5
  • 3
    • 0000115898 scopus 로고
    • Polyamines in food and their consequences for food quality and human health
    • Bardócz S (1995) Polyamines in food and their consequences for food quality and human health. Trends Food Sci Tech 6:341-346
    • (1995) Trends Food Sci Tech , vol.6 , pp. 341-346
    • Bardócz, S.1
  • 4
    • 34548519907 scopus 로고    scopus 로고
    • A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A (1999) A 30 Å 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
  • 5
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment if neurological disorders
    • Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, Mattevi A (2002a) Structure of human monoamine oxidase B, a drug target for the treatment if neurological disorders. Nat Struct Biol 9:22-26
    • (2002) Nat Struct Biol , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubálek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 6
    • 0037025299 scopus 로고    scopus 로고
    • Structure-function relationships in flavoenzyme dependent amine oxidations
    • Binda C, Mattevi A, Edmondson DE (2002b) Structure-function relationships in flavoenzyme dependent amine oxidations. J Biol Chem 277:23973-23976
    • (2002) J Biol Chem , vol.277 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 7
    • 1942436240 scopus 로고    scopus 로고
    • Crystal structure of human monoamine oxidase B, a drug target enzyme monotopically inserted into the mitochondrial outer membrane
    • Binda C, Hubálek F, Li M, Edmondson DE, Mattevi A (2004a) Crystal structure of human monoamine oxidase B, a drug target enzyme monotopically inserted into the mitochondrial outer membrane. FEBS Lett 564:225-228
    • (2004) FEBS Lett , vol.564 , pp. 225-228
    • Binda, C.1    Hubálek, F.2    Li, M.3    Edmondson, D.E.4    Mattevi, A.5
  • 8
    • 12144289182 scopus 로고    scopus 로고
    • Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class
    • Binda C, Hubálek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A (2004b) Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem 47:1767-1774
    • (2004) J Med Chem , vol.47 , pp. 1767-1774
    • Binda, C.1    Hubálek, F.2    Li, M.3    Herzig, Y.4    Sterling, J.5    Edmondson, D.E.6    Mattevi, A.7
  • 9
    • 29744451969 scopus 로고    scopus 로고
    • Binding of rasagiline-related inhibitors to human monoamine oxidases: A kinetic and crystallographic analysis
    • Binda C, Hubálek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A (2005) Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis. J Med Chem 48:8148-8154
    • (2005) J Med Chem , vol.48 , pp. 8148-8154
    • Binda, C.1    Hubálek, F.2    Li, M.3    Herzig, Y.4    Sterling, J.5    Edmondson, D.E.6    Mattevi, A.7
  • 10
  • 11
    • 34248228763 scopus 로고    scopus 로고
    • Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases
    • Casero RA Jr, Marton LJ (2007) Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases. Nat Rev Drug Discov 6:373-390
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 373-390
    • Casero Jr., R.A.1    Marton, L.J.2
  • 12
    • 0016425962 scopus 로고
    • The steady-state kinetics of peroxidase with 2,2′-azino-di-(3- ethylbenzthiazoline-6-sulphonic acid) as chromogen
    • Childs RE, Bardsley WG (1975) The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethylbenzthiazoline-6-sulphonic acid) as chromogen. Biochem J 145:93-103
    • (1975) Biochem J , vol.145 , pp. 93-103
    • Childs, R.E.1    Bardsley, W.G.2
  • 13
    • 24644437716 scopus 로고    scopus 로고
    • Three-dimensional structure of human monoamine oxidase a (MAO A): Relation to the structures of rat MAO a and human MAO B
    • De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A (2005) Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A 102:12684-12689
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 12684-12689
    • De Colibus, L.1    Li, M.2    Binda, C.3    Lustig, A.4    Edmondson, D.E.5    Mattevi, A.6
  • 14
    • 0015501657 scopus 로고
    • Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme
    • Desa RJ (1972) Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme. J Biol Chem 247:5527-5534
    • (1972) J Biol Chem , vol.247 , pp. 5527-5534
    • Desa, R.J.1
  • 15
    • 33644523056 scopus 로고    scopus 로고
    • A chemoenzymatic route to enantiomerically pure cyclic tertiary amines
    • Dunsmore CJ, Carr R, Fleming T, Turner N (2006) A chemoenzymatic route to enantiomerically pure cyclic tertiary amines. J Am Chem Soc 128:2224-2225
    • (2006) J Am Chem Soc , vol.128 , pp. 2224-2225
    • Dunsmore, C.J.1    Carr, R.2    Fleming, T.3    Turner, N.4
  • 16
    • 0031558799 scopus 로고    scopus 로고
    • Competitive inhibition of swine kidney copper amine oxidase by drugs: Amiloride, clonidine, and gabexate mesylate
    • Federico R, Angelini R, Ercolini L, Venturini G, Mattevi A, Ascenzi P (1997) Competitive inhibition of swine kidney copper amine oxidase by drugs: amiloride, clonidine, and gabexate mesylate. Biochem Biophys Res Commun 240:150-152
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 150-152
    • Federico, R.1    Angelini, R.2    Ercolini, L.3    Venturini, G.4    Mattevi, A.5    Ascenzi, P.6
  • 17
    • 0030999852 scopus 로고    scopus 로고
    • Enigmatic gratuitous induction of the covalent flavoprotein vanillyl-alcohol oxidase in Penicillium simplicissimum
    • Fraaije MW, Pikkemaat M, Van Berkel W (1997) Enigmatic gratuitous induction of the covalent flavoprotein vanillyl-alcohol oxidase in Penicillium simplicissimum. Appl Environ Microbiol 63:435-439
    • (1997) Appl Environ Microbiol , vol.63 , pp. 435-439
    • Fraaije, M.W.1    Pikkemaat, M.2    Van Berkel, W.3
  • 18
  • 19
    • 34547122265 scopus 로고    scopus 로고
    • Discovery, characterization and kinetic analysis of an alditol oxidase from Streptomyces coelicolor
    • Heuts DPHM, van Hellemond EW, Janssen DB, Fraaije MW (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
    • Dphm, H.1    Van Hellemond, E.W.2    Janssen, D.B.3    Fraaije, M.W.4
  • 20
    • 0027516803 scopus 로고
    • Putrescine oxidase of Micrococcus rubens: Primary structure and Escherichia coli
    • Ishizuka H, Horinouchi S, Beppu T (1993) Putrescine oxidase of Micrococcus rubens: primary structure and Escherichia coli. J Gen Microbiol 139:425-432
    • (1993) J Gen Microbiol , vol.139 , pp. 425-432
    • Ishizuka, H.1    Horinouchi, S.2    Beppu, T.3
  • 22
    • 0026877727 scopus 로고
    • Enzymes and pathways of polyamine breakdown in microorganisms
    • Large PJ (1992) Enzymes and pathways of polyamine breakdown in microorganisms. FEMS Microbiol Rev 88:249-262
    • (1992) FEMS Microbiol Rev , vol.88 , pp. 249-262
    • Large, P.J.1
  • 23
    • 33645947962 scopus 로고    scopus 로고
    • Functional role of the "aromatic cage" in human monoamine oxidase B: Structures and catalytic properties of Tyr435 mutant proteins
    • Li M, Binda C, Mattevi A, Edmondson DE (2006) Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins. Biochemistry 45:4775-4784
    • (2006) Biochemistry , vol.45 , pp. 4775-4784
    • Li, M.1    Binda, C.2    Mattevi, A.3    Edmondson, D.E.4
  • 24
    • 0031899184 scopus 로고    scopus 로고
    • UGA read-through artifacts-when popular gene expression systems need a pATCH
    • MacBeath G, Kast P (1998) UGA read-through artifacts-when popular gene expression systems need a pATCH. Biotechniques 24:789-794
    • (1998) Biotechniques , vol.24 , pp. 789-794
    • MacBeath, G.1    Kast, P.2
  • 25
    • 0018497710 scopus 로고
    • Substrate specificity and reaction mechanism of putrescine oxidase
    • Okada M, Kawashima S, Imahori K (1979) Substrate specificity and reaction mechanism of putrescine oxidase. J Biochem 86:97-104
    • (1979) J Biochem , vol.86 , pp. 97-104
    • Okada, M.1    Kawashima, S.2    Imahori, K.3
  • 26
    • 0019050214 scopus 로고
    • Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3- dimethylaminopropyl)carbodiimide or metal ions
    • Okada M, Kawashima S, Imahori K (1980) Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. J Biochem 88:481-488
    • (1980) J Biochem , vol.88 , pp. 481-488
    • Okada, M.1    Kawashima, S.2    Imahori, K.3
  • 27
    • 0032914318 scopus 로고    scopus 로고
    • Monoamine oxidase: From genes to behavior
    • Shih JC, Chen K, Ridd MJ (1999) Monoamine oxidase: from genes to behavior. Annu Rev Neurosci 22:197-217
    • (1999) Annu Rev Neurosci , vol.22 , pp. 197-217
    • Shih, J.C.1    Chen, K.2    Ridd, M.J.3
  • 28
    • 0017224897 scopus 로고
    • Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens
    • Swain WF, Desa RJ (1976) Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens. Biochim Biophys Acta 429:331-341
    • (1976) Biochim Biophys Acta , vol.429 , pp. 331-341
    • Swain, W.F.1    Desa, R.J.2
  • 31
    • 0021103515 scopus 로고
    • A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation
    • Wolf P (1983) A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation. Anal Biochem 129:145-155
    • (1983) Anal Biochem , vol.129 , pp. 145-155
    • Wolf, P.1


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