메뉴 건너뛰기




Volumn 38, Issue 1, 2010, Pages 247-255

D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637

Author keywords

Bacterial respiration; D Amino acid dehydrogenase; D Proline; Gene cloning; Helicobacter pylori

Indexed keywords

DEXTRO AMINO ACID DEHYDROGENASE; OXIDOREDUCTASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 76449095058     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-009-0240-0     Document Type: Article
Times cited : (32)

References (25)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D 942051
    • MM Bradford 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding Anal Biochem 72 248 254 10.1016/0003-2697(76)90527-3 10.1016/0003-2697(76)90527- 3 1:CAS:528:DyaE28XksVehtrY%3D 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 50549204004 scopus 로고
    • D-Amino acid oxidase II. Specificity, competitive inhibitions and reaction sequence
    • 1:CAS:528:DyaF2MXotlyrsA%3D%3D
    • M Dixon K Kleppe 1965 d-Amino acid oxidase II. Specificity, competitive inhibitions and reaction sequence Biochim Biophys Acta 96 368 382 1:CAS:528:DyaF2MXotlyrsA%3D%3D
    • (1965) Biochim Biophys Acta , vol.96 , pp. 368-382
    • Dixon, M.1    Kleppe, K.2
  • 3
    • 0030725576 scopus 로고    scopus 로고
    • Helicobacter pylori
    • 1:CAS:528:DyaK2sXmvFyhu7c%3D 9336670
    • BE Dunn H Cohen MJ Blaser 1997 Helicobacter pylori Clin Microbiol Rev 10 720 741 1:CAS:528:DyaK2sXmvFyhu7c%3D 9336670
    • (1997) Clin Microbiol Rev , vol.10 , pp. 720-741
    • Dunn, B.E.1    Cohen, H.2    Blaser, M.J.3
  • 4
    • 0030448047 scopus 로고    scopus 로고
    • Microbial D-amino acid oxidases (EC 1.4.3.3)
    • DOI 10.1111/j.1749-6632.1996.tb33274.x
    • L Fischer M Gabler R Horner F Wagner 1996 Microbial d-amino acid oxidases (EC 1.4.3.3) Ann NY Acad Sci 799 683 688 10.1111/j.1749-6632.1996.tb33274.x 1:CAS:528:DyaK2sXhtVems7w%3D 8992943 (Pubitemid 27029530)
    • (1996) Annals of the New York Academy of Sciences , vol.799 , pp. 683-688
    • Fischer, L.1    Gabler, M.2    Horner, R.3    Wagner, F.4
  • 5
    • 0017181918 scopus 로고
    • Biochemical, genetic, and regulatory studies of alanine catabolism in scherichia coli K12
    • 10.1007/BF00332894 10.1007/BF00332894 1:CAS:528:DyaE2sXjvF2rsA%3D%3D 13292
    • FCH Franklin WA Venables 1976 Biochemical, genetic, and regulatory studies of alanine catabolism in scherichia coli K12 Mol Gen Genet 149 229 237 10.1007/BF00332894 10.1007/BF00332894 1:CAS:528:DyaE2sXjvF2rsA%3D%3D 13292
    • (1976) Mol Gen Genet , vol.149 , pp. 229-237
    • Franklin, F.C.H.1    Venables, W.A.2
  • 6
    • 70449144013 scopus 로고
    • The sulfhydryl character of d-amino acid oxidase
    • WR Frisell L Hellerman 1956 The sulfhydryl character of d-amino acid oxidase J Biol Chem 225 53 62
    • (1956) J Biol Chem , vol.225 , pp. 53-62
    • Frisell, W.R.1    Hellerman, L.2
  • 7
    • 0343478442 scopus 로고
    • Flavoenzyme catalysis. Substrate-competitive inhibition of d-amino acid oxidase
    • 1:CAS:528:DyaG2sXhslKrsw%3D%3D 13376578
    • WR Frisell HJ Lowe L Hellerman 1956 Flavoenzyme catalysis. Substrate-competitive inhibition of d-amino acid oxidase J Biol Chem 223 75 83 1:CAS:528:DyaG2sXhslKrsw%3D%3D 13376578
    • (1956) J Biol Chem , vol.223 , pp. 75-83
    • Frisell, W.R.1    Lowe, H.J.2    Hellerman, L.3
  • 8
    • 0023657734 scopus 로고
    • Molecular cloning and sequence analysis of cDNAs encoding porcine kidney d-amino acid oxidase
    • 10.1021/bi00386a054 10.1021/bi00386a054 1:CAS:528:DyaL2sXkvFWju7g%3D 2888479
    • K Fukui F Watanabe T Shibata Y Miyake 1987 Molecular cloning and sequence analysis of cDNAs encoding porcine kidney d-amino acid oxidase Biochemistry 26 3612 3618 10.1021/bi00386a054 10.1021/bi00386a054 1:CAS:528:DyaL2sXkvFWju7g%3D 2888479
    • (1987) Biochemistry , vol.26 , pp. 3612-3618
    • Fukui, K.1    Watanabe, F.2    Shibata, T.3    Miyake, Y.4
  • 9
    • 0031733223 scopus 로고    scopus 로고
    • The physiology and metabolism of the human gastric pathogen Helicobacter pylori
    • 10.1016/S0065-2911(08)60131-9 10.1016/S0065-2911(08)60131-9
    • DJ Kelly 1998 The physiology and metabolism of the human gastric pathogen Helicobacter pylori Adv Microb Physiol 44 137 189 10.1016/S0065-2911(08)60131-9 10.1016/S0065-2911(08)60131-9
    • (1998) Adv Microb Physiol , vol.44 , pp. 137-189
    • Kelly, D.J.1
  • 10
    • 32444440473 scopus 로고    scopus 로고
    • Oxygen reactivity of PutA from Helicobacter species and proline-linked oxidative stress
    • DOI 10.1128/JB.188.4.1227-1235.2006
    • N Krishnan DB Becker 2006 Oxygen reactivity of PutA from Helicobacter species and proline-linked oxidative stress J Bacteriol 188 1227 1235 10.1128/JB.188.4.1227-1235.2006 10.1128/JB.188.4.1227-1235.2006 1:CAS:528:DC%2BD28Xhs1Gmurc%3D 16452403 (Pubitemid 43228654)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1227-1235
    • Krishnan, N.1    Becker, D.F.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • 10.1038/227680a0 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the bacteriophage T4 Nature 227 680 685 10.1038/227680a0 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0028294870 scopus 로고
    • Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of d-amino acid dehydrogenase and the catabolic alanine racemase
    • 7906689
    • M Łobocka J Henning J Wild T Kłopotowski 1994 Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of d-amino acid dehydrogenase and the catabolic alanine racemase J Bacteriol 176 1500 1510 7906689
    • (1994) J Bacteriol , vol.176 , pp. 1500-1510
    • Łobocka, M.1    Henning, J.2    Wild, J.3    Kłopotowski, T.4
  • 13
    • 0014271103 scopus 로고
    • Oxidation of d-amino acids by a particulate enzyme from Pseudomonas aeruginosa
    • 1:CAS:528:DyaF1cXptlWntA%3D%3D 4384679
    • VP Marshall JR Sokatch 1968 Oxidation of d-amino acids by a particulate enzyme from Pseudomonas aeruginosa J Bacteriol 95 1419 1425 1:CAS:528: DyaF1cXptlWntA%3D%3D 4384679
    • (1968) J Bacteriol , vol.95 , pp. 1419-1425
    • Marshall, V.P.1    Sokatch, J.R.2
  • 14
    • 0019805440 scopus 로고
    • Enzymatic properties of the purified putA protein from Salmonella typhimurium
    • 1:CAS:528:DyaL3MXls1Cnu7c%3D 6270101
    • R Menzel J Roth 1981 Enzymatic properties of the purified putA protein from Salmonella typhimurium J Biol Chem 256 9762 9766 1:CAS:528: DyaL3MXls1Cnu7c%3D 6270101
    • (1981) J Biol Chem , vol.256 , pp. 9762-9766
    • Menzel, R.1    Roth, J.2
  • 15
    • 0042424963 scopus 로고    scopus 로고
    • L-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: Correlation between in vitro and in vivo amino acid levels
    • 10.1099/mic.0.26203-0 10.1099/mic.0.26203-0 1:CAS:528: DC%2BD3sXmslaqsLw%3D
    • K Nagata Y Nagata T Sato A Fujino K Nakajima T Tamura 2003 l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels Microbiol 149 2023 2030 10.1099/mic.0.26203-0 10.1099/mic.0.26203-0 1:CAS:528:DC%2BD3sXmslaqsLw%3D
    • (2003) Microbiol , vol.149 , pp. 2023-2030
    • Nagata, K.1    Nagata, Y.2    Sato, T.3    Fujino, A.4    Nakajima, K.5    Tamura, T.6
  • 16
    • 33845251139 scopus 로고    scopus 로고
    • High concentrations of D-amino acids in human gastric juice
    • DOI 10.1007/s00726-006-0262-9, Special Issue: Focus on Biologically Active D-Amino Acids
    • Y Nagata T Sato N Enomoto Y Isii K Sasaki T Yamada 2007 High concentrations of d-amino acids in human gastric juice Amino Acids 32 137 140 10.1007/s00726-006-0262-9 10.1007/s00726-006-0262-9 1:CAS:528:DC%2BD28Xht1Ogs73E 16583309 (Pubitemid 44866580)
    • (2007) Amino Acids , vol.32 , Issue.1 , pp. 137-140
    • Nagata, Y.1    Sato, T.2    Enomoto, N.3    Ishii, Y.4    Sasaki, K.5    Yamada, T.6
  • 17
    • 0018821298 scopus 로고
    • Purification and properties of d-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli
    • 1:CAS:528:DyaL3cXks1CnsL4%3D 6102989
    • PJ Olsiewski CJ Kaczorowski CT Walsh 1980 Purification and properties of d-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli J Biol Chem 255 4487 4494 1:CAS:528:DyaL3cXks1CnsL4%3D 6102989
    • (1980) J Biol Chem , vol.255 , pp. 4487-4494
    • Olsiewski, P.J.1    Kaczorowski, C.J.2    Walsh, C.T.3
  • 18
    • 0015863560 scopus 로고
    • D-Alanine oxidase from Escherichia coli: Participation in the oxidation of l-alanine
    • 1:CAS:528:DyaE3sXks1eisbY%3D 4146873
    • RP Raunio LP Straus WT Jenkins 1973 d-Alanine oxidase from Escherichia coli: Participation in the oxidation of l-alanine J Bacteriol 115 567 573 1:CAS:528:DyaE3sXks1eisbY%3D 4146873
    • (1973) J Bacteriol , vol.115 , pp. 567-573
    • Raunio, R.P.1    Straus, L.P.2    Jenkins, W.T.3
  • 19
    • 0020479451 scopus 로고
    • The primary structure of d-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence
    • 1:CAS:528:DyaL38XlsFyksrc%3D 6124543
    • S Ronchi L Minchiotti M Galliano B Curti RP Swenson CH Williams Jr V Massey 1982 The primary structure of d-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence J Biol Chem 257 8824 8834 1:CAS:528:DyaL38XlsFyksrc%3D 6124543
    • (1982) J Biol Chem , vol.257 , pp. 8824-8834
    • Ronchi, S.1    Minchiotti, L.2    Galliano, M.3    Curti, B.4    Swenson, R.P.5    Williams Jr, C.H.6    Massey, V.7
  • 20
    • 33846259335 scopus 로고    scopus 로고
    • Alanine racemase from Helicobacter pylori NCTC 11637:Purification, characterization and gene cloning
    • DOI 10.1016/j.lfs.2006.11.005, PII S0024320506008605
    • M Saito K Nishimura Y Hasegawa T Shinohara S Wakabayashi T Kurihara M Ishizuka Y Nagata 2007 Alanine racemase from Helicobacter pylori NCTC 11637: purification, characterization and gene cloning Life Sci 80 788 794 10.1016/j.lfs.2006.11.005 10.1016/j.lfs.2006.11.005 1:CAS:528: DC%2BD2sXntl2itg%3D%3D 17196222 (Pubitemid 46108001)
    • (2007) Life Sciences , vol.80 , Issue.8 , pp. 788-794
    • Saito, M.1    Nishimura, K.2    Hasegawa, Y.3    Shinohara, T.4    Wakabayashi, S.5    Kurihara, T.6    Ishizuka, M.7    Nagata, Y.8
  • 21
    • 0037066754 scopus 로고    scopus 로고
    • Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase
    • DOI 10.1074/jbc.M112272200
    • T Satomura R Kawakami H Sakuraba T Ohshima 2002 Dye-linked d-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase J Biol Chem 277 12861 12867 10.1074/jbc.M112272200 10.1074/jbc.M112272200 1:CAS:528:DC%2BD38XivFSjs7c%3D 11823469 (Pubitemid 34952651)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12861-12867
    • Satomura, T.1    Kawakami, R.2    Sakuraba, H.3    Ohshima, T.4
  • 22
    • 0018168502 scopus 로고
    • Membrane-bound proline dehydrogenase from Escherichia coli
    • 1:CAS:528:DyaE1cXlslGmsL0%3D 355248
    • RC Scarpulla RL Soffer 1978 Membrane-bound proline dehydrogenase from Escherichia coli J Biol Chem 253 5997 6001 1:CAS:528:DyaE1cXlslGmsL0%3D 355248
    • (1978) J Biol Chem , vol.253 , pp. 5997-6001
    • Scarpulla, R.C.1    Soffer, R.L.2
  • 23
    • 0028064605 scopus 로고
    • A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach
    • 1:CAS:528:DyaK2cXmsFSqur0%3D 8039935
    • M Tsuda M Karita MG Morshed K Okita T Nakazawa 1994 A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach Infect Immun 62 3586 3589 1:CAS:528:DyaK2cXmsFSqur0%3D 8039935
    • (1994) Infect Immun , vol.62 , pp. 3586-3589
    • Tsuda, M.1    Karita, M.2    Morshed, M.G.3    Okita, K.4    Nakazawa, T.5
  • 24
    • 0014011413 scopus 로고
    • D-Amino acid dehydrogenases of Pseudomonas fluorescence
    • 1:CAS:528:DyaF28XkslCqsrg%3D 5925166
    • K Tsukada 1966 d-Amino acid dehydrogenases of Pseudomonas fluorescence J Biol Chem 241 4522 4528 1:CAS:528:DyaF28XkslCqsrg%3D 5925166
    • (1966) J Biol Chem , vol.241 , pp. 4522-4528
    • Tsukada, K.1
  • 25
    • 0016015888 scopus 로고
    • D-Amino acid dehydrogenase: The enzyme of the first step of d-histidine and d-methionine racemisation in Salmonella typhimurium
    • 10.1007/BF02654486 10.1007/BF02654486 1:CAS:528:DyaE2cXltFKqur8%3D 4150767
    • J Wild W Walczac K Krajewska-Grynkiewicz T Klopotowski 1974 d-Amino acid dehydrogenase: the enzyme of the first step of d-histidine and d-methionine racemisation in Salmonella typhimurium Mol Gen Genet 128 131 146 10.1007/BF02654486 10.1007/BF02654486 1:CAS:528:DyaE2cXltFKqur8%3D 4150767
    • (1974) Mol Gen Genet , vol.128 , pp. 131-146
    • Wild, J.1    Walczac, W.2    Krajewska-Grynkiewicz, K.3    Klopotowski, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.