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Volumn 4, Issue , 2004, Pages

Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

AMINOOXYACETIC ACID; AMINOTRANSFERASE; ANTIMYCOBACTERIAL AGENT; BENZYLOXYAMINE; CANALINE; GLUTAMIC ACID; HYDROXYLAMINE; HYDROXYLAMINOSULFONIC ACID; ISOLEUCINE; KETOMETHIOBUTYRATE; KETONE DERIVATIVE; LEUCINE; METHIONINE; METHOXYAMINE; O ALLYLHYDROXYLAMINE; O ETHYLHYDROXYLAMINE; O NITROBENZYLHYDROXYLAMINE; O PENTAFLUOROBENZYLHYDROXYLAMINE; O TERT BUTYLDIMETHYLSILYLHYDROXYLAMINE; O TERT BUTYLHYDROXYLAMINE; O TETRAHYDROPYRANYLHYDROXYLAMINE; PHENYLALANINE; UNCLASSIFIED DRUG; VALINE;

EID: 8844278368     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-4-39     Document Type: Article
Times cited : (34)

References (55)
  • 1
    • 0033581124 scopus 로고    scopus 로고
    • Consensus statement. Global burden of tuberculosis: Estimated incidence, prevalence, and mortality by country
    • WHO Global Surveillance and Monitoring Project
    • Dye C, Scheele S, Dolin P, Pathania V, Raviglione MC: Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project. JAMA 1999, 282:677-86.
    • (1999) JAMA , vol.282 , pp. 677-686
    • Dye, C.1    Scheele, S.2    Dolin, P.3    Pathania, V.4    Raviglione, M.C.5
  • 2
    • 0025099504 scopus 로고
    • Selective killing of Klebsiella pneumoniae by 5- trifluoromethylthioribose. Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase
    • Gianotti AJ, Tower PA, Sheley JH, Conte PA, Spiro C, Ferro AJ, Fitchen JH, Riscoe MK: Selective killing of Klebsiella pneumoniae by 5- trifluoromethylthioribose. Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase. J Biol Chem 1990, 265:831-7.
    • (1990) J Biol Chem , vol.265 , pp. 831-837
    • Gianotti, A.J.1    Tower, P.A.2    Sheley, J.H.3    Conte, P.A.4    Spiro, C.5    Ferro, A.J.6    Fitchen, J.H.7    Riscoe, M.K.8
  • 3
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton LJ, Pegg AE: Polyamines as targets for therapeutic intervention. Ann Rev Pharmacoland Toxicol 1995, 35:55-91.
    • (1995) Ann Rev Pharmacoland Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 5
    • 0029891413 scopus 로고    scopus 로고
    • Affinity purification of 5-methylthioribose kinase and 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae
    • Cornell KA, Winter RW, Tower PA, Riscoe MK: Affinity purification of 5-methylthioribose kinase and 5- methylthioadenosine/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae. Biochem J 1996, 317:285-90.
    • (1996) Biochem J , vol.317 , pp. 285-290
    • Cornell, K.A.1    Winter, R.W.2    Tower, P.A.3    Riscoe, M.K.4
  • 6
    • 0023718385 scopus 로고
    • Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae
    • Furfine ES, Abeles RH: Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J Biol Chem 1988, 263:9598-606.
    • (1988) J Biol Chem , vol.263 , pp. 9598-9606
    • Furfine, E.S.1    Abeles, R.H.2
  • 7
    • 0033028593 scopus 로고    scopus 로고
    • Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae
    • Heilbronn J, Wilson J, Berger BJ: Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J Bacteriol 1999, 181:1739-47.
    • (1999) J Bacteriol , vol.181 , pp. 1739-1747
    • Heilbronn, J.1    Wilson, J.2    Berger, B.J.3
  • 8
    • 0027367423 scopus 로고
    • Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
    • Myers RW, Wray JW, Fish S, Abeles RH: Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J Biol Chem 1993, 268:24785-91.
    • (1993) J Biol Chem , vol.268 , pp. 24785-24791
    • Myers, R.W.1    Wray, J.W.2    Fish, S.3    Abeles, R.H.4
  • 9
    • 0021099574 scopus 로고
    • Methionine synthesis from 5′-S-Methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose
    • Trackman PC, Abeles RH: Methionine synthesis from 5′-S- Methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose. J Biol Chem 1983, 258:6717-20.
    • (1983) J Biol Chem , vol.258 , pp. 6717-6720
    • Trackman, P.C.1    Abeles, R.H.2
  • 10
    • 0027378886 scopus 로고
    • A bacterial enzyme that catalyzes formation of carbon monoxide
    • Wray JW, Abeles RH: A bacterial enzyme that catalyzes formation of carbon monoxide. J Biol Chem 1993, 268:21466-9.
    • (1993) J Biol Chem , vol.268 , pp. 21466-21469
    • Wray, J.W.1    Abeles, R.H.2
  • 11
    • 0028850881 scopus 로고
    • The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases
    • Wray JW, Abeles RH: The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J Biol Chem 1995, 270:3147-53.
    • (1995) J Biol Chem , vol.270 , pp. 3147-3153
    • Wray, J.W.1    Abeles, R.H.2
  • 12
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO
    • Ashida H, Saito Y, Kojima C, Kobayashi K, Ogasawara N, Yokota A: A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 2003, 302:286-90.
    • (2003) Science , vol.302 , pp. 286-290
    • Ashida, H.1    Saito, Y.2    Kojima, C.3    Kobayashi, K.4    Ogasawara, N.5    Yokota, A.6
  • 13
    • 0036202171 scopus 로고    scopus 로고
    • Prediction of gene function in methylthioadenosine recycling from regulatory signals
    • Murphy BA, Grundy FJ, Henkin TM: Prediction of gene function in methylthioadenosine recycling from regulatory signals. J Bacteriol 2002, 184:2314-8.
    • (2002) J Bacteriol , vol.184 , pp. 2314-2318
    • Murphy, B.A.1    Grundy, F.J.2    Henkin, T.M.3
  • 14
    • 19044362589 scopus 로고    scopus 로고
    • The methionine salvage pathway in Bacillus subtilis
    • Sekowska A, Danchin A: The methionine salvage pathway in Bacillus subtilis. BMC Microbiol 2002, 2:8.
    • (2002) BMC Microbiol , vol.2 , pp. 8
    • Sekowska, A.1    Danchin, A.2
  • 15
    • 0019945865 scopus 로고
    • Identification of 2-keto-4-methylthiobutyrate as an intermediate compound in methionine synthesis from 5′-methylthioadenosine
    • Backlund PS Jr, Chang CP, Smith RA: Identification of 2-keto-4-methylthiobutyrate as an intermediate compound in methionine synthesis from 5′-methylthioadenosine. J Biol Chem 1982, 257:4196-202.
    • (1982) J Biol Chem , vol.257 , pp. 4196-4202
    • Backlund Jr., P.S.1    Chang, C.P.2    Smith, R.A.3
  • 16
    • 0037384217 scopus 로고    scopus 로고
    • Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
    • Berger BJ, English S, Chan G, Knodel MH: Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J Bacteriol 2003, 185:2418-31.
    • (2003) J Bacteriol , vol.185 , pp. 2418-2431
    • Berger, B.J.1    English, S.2    Chan, G.3    Knodel, M.H.4
  • 17
    • 0034932250 scopus 로고    scopus 로고
    • Methionine regeneration and aspartate aminotransferase in parasitic protozoa
    • Berger LC, Wilson J, Wood P, Berger BJ: Methionine regeneration and aspartate aminotransferase in parasitic protozoa. J Bacteriol 2001, 183:4421-34.
    • (2001) J Bacteriol , vol.183 , pp. 4421-4434
    • Berger, L.C.1    Wilson, J.2    Wood, P.3    Berger, B.J.4
  • 18
    • 0021187425 scopus 로고
    • Characterization of a defect in the pathway for converting 5′-deoxy-5′- methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma
    • Ghoda LY, Savarese TM, Dexter DL, Parks RE Jr, Trackman PC, Abeles RH: Characterization of a defect in the pathway for converting 5′-deoxy- 5′- methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma. J Biol Chem 1984, 259:6715-9.
    • (1984) J Biol Chem , vol.259 , pp. 6715-6719
    • Ghoda, L.Y.1    Savarese, T.M.2    Dexter, D.L.3    Parks Jr., R.E.4    Trackman, P.C.5    Abeles, R.H.6
  • 19
    • 9344235427 scopus 로고    scopus 로고
    • Cloning and characterization of the metE gene encoding S- adenosylmethionine synthetase from Bacillus subtilis
    • Yocum RR, Perkins JB, Howitt CL, Pero J: Cloning and characterization of the metE gene encoding S- adenosylmethionine synthetase from Bacillus subtilis. J Bacteriol 1996, 178:4604-10.
    • (1996) J Bacteriol , vol.178 , pp. 4604-4610
    • Yocum, R.R.1    Perkins, J.B.2    Howitt, C.L.3    Pero, J.4
  • 21
    • 2942702220 scopus 로고    scopus 로고
    • Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis
    • Berger BJ, Knodel MH: Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis. BMC Microbiol 2003, 3:12.
    • (2003) BMC Microbiol , vol.3 , pp. 12
    • Berger, B.J.1    Knodel, M.H.2
  • 22
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius JN: Structure, evolution and action of vitamin B6-dependent enzymes. Curr Opin Struct Biol 1998, 8:759-69.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 24
    • 0035954395 scopus 로고    scopus 로고
    • Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2- methylleucine: Induced fit and substrate recognition of the enzyme
    • Okada K, Hirotsu K, Hayashi H, Kagamiyama H: Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2- methylleucine: induced fit and substrate recognition of the enzyme. Biochemistry 2001, 40:7453-63.
    • (2001) Biochemistry , vol.40 , pp. 7453-7463
    • Okada, K.1    Hirotsu, K.2    Hayashi, H.3    Kagamiyama, H.4
  • 25
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A: A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J 1974, 137:143-4.
    • (1974) Biochem J , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 26
    • 0025295941 scopus 로고
    • DL-canaline and 5-fluoromethylornithine. Comparison of two inactivators of ornithine aminotransferase
    • Bolkenius FN, Knodgen B, Seiler N: DL-canaline and 5- fluoromethylornithine. Comparison of two inactivators of ornithine aminotransferase. Biochem J 1990, 268:409-14.
    • (1990) Biochem J , vol.268 , pp. 409-414
    • Bolkenius, F.N.1    Knodgen, B.2    Seiler, N.3
  • 27
    • 0030915618 scopus 로고    scopus 로고
    • L-canaline: A potent antimetabolite and anticancer agent from leguminous plants
    • Rosenthal GA: L-canaline: a potent antimetabolite and anticancer agent from leguminous plants. Life Sci 1997, 60:1635-41.
    • (1997) Life Sci , vol.60 , pp. 1635-1641
    • Rosenthal, G.A.1
  • 28
    • 0029845884 scopus 로고    scopus 로고
    • Structure-activity studies of L-canaline-mediated inhibition of porcine alanine aminotransferase
    • Worthen DR, Ratliff DK, Rosenthal GA, Trifonov L, Crooks PA: Structure-activity studies of L-canaline-mediated inhibition of porcine alanine aminotransferase. Chem Res Toxicol 1996, 9:1293-7.
    • (1996) Chem Res Toxicol , vol.9 , pp. 1293-1297
    • Worthen, D.R.1    Ratliff, D.K.2    Rosenthal, G.A.3    Trifonov, L.4    Crooks, P.A.5
  • 29
    • 0037133580 scopus 로고    scopus 로고
    • Complex pattern of Mycobacterium marinum gene expression during long-term granulomatous infection
    • Chan K, Knaak T, Satkamp L, Humbert O, Falkow S, Ramakrishnan L: Complex pattern of Mycobacterium marinum gene expression during long-term granulomatous infection. Proc Nat Acad Sci USA 2002, 99:3920-5.
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 3920-3925
    • Chan, K.1    Knaak, T.2    Satkamp, L.3    Humbert, O.4    Falkow, S.5    Ramakrishnan, L.6
  • 30
    • 0033836277 scopus 로고    scopus 로고
    • Antimalarial activities of aminooxy compounds
    • Berger BJ: Antimalarial activities of aminooxy compounds. Antimicrob Ag Chemother 2000, 44:2540-2.
    • (2000) Antimicrob Ag Chemother , vol.44 , pp. 2540-2542
    • Berger, B.J.1
  • 31
    • 0036785129 scopus 로고    scopus 로고
    • Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: Ketimine and pyridoxamine phosphate forms
    • Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry 2002, 41:11592-601.
    • (2002) Biochemistry , vol.41 , pp. 11592-11601
    • Yennawar, N.H.1    Conway, M.E.2    Yennawar, H.P.3    Farber, G.K.4    Hutson, S.M.5
  • 32
    • 0017091667 scopus 로고
    • Reactivity of the phosphopyridoxal groups of cystathionase
    • Beeler T, Churchich JE: Reactivity of the phosphopyridoxal groups of cystathionase. J Biol Chem 1976, 251:5267-71.
    • (1976) J Biol Chem , vol.251 , pp. 5267-5271
    • Beeler, T.1    Churchich, J.E.2
  • 33
    • 0032468851 scopus 로고    scopus 로고
    • Methionine formation from alphaketomethiobutyrate in the trypanosomatid Crithidia fasciculata
    • Berger BJ, Dai WW, Wilson J: Methionine formation from alphaketomethiobutyrate in the trypanosomatid Crithidia fasciculata. FEMS Microbiol Letts 1998, 165:305-12.
    • (1998) FEMS Microbiol Letts , vol.165 , pp. 305-312
    • Berger, B.J.1    Dai, W.W.2    Wilson, J.3
  • 34
    • 0023023318 scopus 로고
    • Susceptibility testing of slowly growing mycobacteria by a microdilution MIC method with 7H9 broth
    • Wallace RJ, Nash DR, Steele LC, Steingrube V: Susceptibility testing of slowly growing mycobacteria by a microdilution MIC method with 7H9 broth. J Clin Microbiol 1986, 24:976-981.
    • (1986) J Clin Microbiol , vol.24 , pp. 976-981
    • Wallace, R.J.1    Nash, D.R.2    Steele, L.C.3    Steingrube, V.4
  • 35
    • 84872277786 scopus 로고
    • Bacteriological study of cabroxymethoxylamine hemichloride
    • Favour CB: Bacteriological study of cabroxymethoxylamine hemichloride. J Bacteriol 1948, 55:1-9.
    • (1948) J Bacteriol , vol.55 , pp. 1-9
    • Favour, C.B.1
  • 36
    • 0040929558 scopus 로고
    • The antimicrobial properties of some alpha-amino-oxy-acids, alpha-amino-oxyhydrazides, alkoxyamines, alkoxydiguanides and their derivatives
    • Price SA, Mamalis P, McHale D, Green J: The antimicrobial properties of some alpha-amino-oxy-acids, alpha-amino-oxyhydrazides, alkoxyamines, alkoxydiguanides and their derivatives. Bri J Pharmchemother 1960, 15:243-246.
    • (1960) Bri J Pharmchemother , vol.15 , pp. 243-246
    • Price, S.A.1    Mamalis, P.2    McHale, D.3    Green, J.4
  • 37
    • 37049056488 scopus 로고
    • Amino-oxy-derivatives. Part I. Some α-amino-oxy-acids and α-amino-oxy-hydrazides
    • McHale D, Green J, Mamalis P: Amino-oxy-derivatives. Part I. Some α-amino-oxy-acids and α-amino-oxy-hydrazides. J Chem Soc 1960, 1960:225-229.
    • (1960) J Chem Soc , vol.1960 , pp. 225-229
    • McHale, D.1    Green, J.2    Mamalis, P.3
  • 38
    • 0015227015 scopus 로고
    • Alpha-Aminooxy-acid derivatives with potent antituberculotic effect
    • Kisfaludy L, Dancsi L, Patthy A, Fekete G, Szabo I: alpha-Aminooxy-acid derivatives with potent antituberculotic effect. Experientia 1971, 27:1055-1056.
    • (1971) Experientia , vol.27 , pp. 1055-1056
    • Kisfaludy, L.1    Dancsi, L.2    Patthy, A.3    Fekete, G.4    Szabo, I.5
  • 39
    • 0344549320 scopus 로고
    • Amino-oxy-derivatives. Part II. Some derivatives of N-hydroxydiguanide
    • Mamalis P, Green J, McHale D: Amino-oxy-derivatives. Part II. Some derivatives of N-hydroxydiguanide. J Chem Soc 1960, 1960:229-238.
    • (1960) J Chem Soc , vol.1960 , pp. 229-238
    • Mamalis, P.1    Green, J.2    McHale, D.3
  • 41
    • 0023121210 scopus 로고
    • Ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase and arginine decarboxylase from Mycobacterium bovis (BCG)
    • Paulin L, Brander E, Poso H: Ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase and arginine decarboxylase from Mycobacterium bovis (BCG). Experientia 1987, 43:174-6.
    • (1987) Experientia , vol.43 , pp. 174-176
    • Paulin, L.1    Brander, E.2    Poso, H.3
  • 44
    • 0017076160 scopus 로고
    • Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands
    • Chou TC: Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands. J Theor Biol 1976, 59:253-76.
    • (1976) J Theor Biol , vol.59 , pp. 253-276
    • Chou, T.C.1
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 1994, 22:4673-80.
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0002051540 scopus 로고    scopus 로고
    • Bioedit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA: Bioedit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl Acids Symp Ser 1999, 41:95-98.
    • (1999) Nucl Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 48
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (version 3.2)
    • Felsenstein J: PHYLIP - phylogeny inference package (version 3.2). Cladistics 1989, 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 49
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M: The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4:406-25.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 50
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page RD: TreeView: an application to display phylogenetic trees on personal computers. Computer Appl Biosci 1996, 12:357-8.
    • (1996) Computer Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 54
    • 0030901404 scopus 로고    scopus 로고
    • Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)
    • Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta 1997, 1339:9-13.
    • (1997) Biochim Biophys Acta , vol.1339 , pp. 9-13
    • Bledsoe, R.K.1    Dawson, P.A.2    Hutson, S.M.3
  • 55
    • 0021909278 scopus 로고
    • Branched-chain amino acid aminotransferase of Escherichia coli: Nucleotide sequence of the ilvE gene and the deduced amino acid sequence
    • Kuramitsu S, Ogawa T, Ogawa H, Kagamiyama H: Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence. J Biochem 1985, 97:993-9.
    • (1985) J Biochem , vol.97 , pp. 993-999
    • Kuramitsu, S.1    Ogawa, T.2    Ogawa, H.3    Kagamiyama, H.4


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