메뉴 건너뛰기




Volumn 186, Issue 6, 2004, Pages 1890-1892

The eutD Gene of Salmonella enterica Encodes a Protein with Phosphotransacetylase Enzyme Activity

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETYL COENZYME A; BACTERIAL ENZYME; CARBON; ETHANOLAMINE; PHOSPHATE ACETYLTRANSFERASE; PROPIONIC ACID; PROPYLENE GLYCOL; PROTEIN EUTD; UNCLASSIFIED DRUG;

EID: 1542286908     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.6.1890-1892.2004     Document Type: Article
Times cited : (32)

References (25)
  • 1
    • 0000244215 scopus 로고
    • Ethanolamine ammonia-lyase
    • D. Dolphin (ed.). John Wiley & Sons, New York, N.Y.
    • 12, vol. 2. John Wiley & Sons, New York, N.Y.
    • (1982) 12 , vol.2 , pp. 263-288
    • Babior, B.M.1
  • 2
    • 0033592313 scopus 로고    scopus 로고
    • Hydrogen atom exchange between 5′-deoxyadenosine and hydroxyethylhydrazine during the single turnover inactivation of ethanolamine ammonia-lyase
    • Bandarian, V., R. R. Poyner, and G. H. Reed. 1999. Hydrogen atom exchange between 5′-deoxyadenosine and hydroxyethylhydrazine during the single turnover inactivation of ethanolamine ammonia-lyase. Biochemistry 38:12403-12407.
    • (1999) Biochemistry , vol.38 , pp. 12403-12407
    • Bandarian, V.1    Poyner, R.R.2    Reed, G.H.3
  • 3
    • 0037047017 scopus 로고    scopus 로고
    • Analysis of the electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol
    • Bandarian, V., and G. H. Reed. 2002. Analysis of the electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol. Biochemistry 41:8580-8588.
    • (2002) Biochemistry , vol.41 , pp. 8580-8588
    • Bandarian, V.1    Reed, G.H.2
  • 5
    • 0018256258 scopus 로고
    • 12-dependent ethanolamine ammonialyase and its concerted induction in Escherichia coli
    • 12-dependent ethanolamine ammonialyase and its concerted induction in Escherichia coli. Biochem. J. 176:751-757.
    • (1978) Biochem. J. , vol.176 , pp. 751-757
    • Blackwell, C.M.1    Turner, J.M.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-255.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-255
    • Bradford, M.M.1
  • 8
    • 0016593454 scopus 로고
    • 12-dependent enzyme ethanolamine deaminase in Salmonella
    • 12-dependent enzyme ethanolamine deaminase in Salmonella. Nature 254:150-151.
    • (1975) Nature , vol.254 , pp. 150-151
    • Chang, G.W.1    Chang, J.T.2
  • 9
    • 0025286022 scopus 로고
    • Cloning, sequencing and expression of the genes encoding the adenosylco-balamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium
    • Faust, L. P., J. A. Connor, D. M. Roof, J. A. Hoch, and B. M. Babior. 1990. Cloning, sequencing and expression of the genes encoding the adenosylco-balamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium. J. Biol. Chem. 265:12462-12466.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12462-12466
    • Faust, L.P.1    Connor, J.A.2    Roof, D.M.3    Hoch, J.A.4    Babior, B.M.5
  • 10
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • Frey, P. A. 2001. Radical mechanisms of enzymatic catalysis. Annu. Rev. Biochem. 70:121-148.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 11
    • 0034333084 scopus 로고    scopus 로고
    • The synthetase domains of cobalamin biosynthesis amidotransferases CobB and CobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase
    • Galperin, M. Y., and N. V. Grishin. 2000. The synthetase domains of cobalamin biosynthesis amidotransferases CobB and CobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Proteins 41:238-247.
    • (2000) Proteins , vol.41 , pp. 238-247
    • Galperin, M.Y.1    Grishin, N.V.2
  • 12
    • 0042389658 scopus 로고    scopus 로고
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J. Bacteriol. 185:5086-5095.
    • (2003) J. Bacteriol. , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 13
    • 0036178889 scopus 로고    scopus 로고
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J. Bacteriol. 184:1253-1261.
    • (2002) J. Bacteriol. , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 14
    • 0022578928 scopus 로고
    • Determination of short-chain acyl-coenzyme A esters by high-performance liquid chromatography
    • Hosokawa, Y., Y. Shimomura, R. A. Harris, and T. Ozawa. 1986. Determination of short-chain acyl-coenzyme A esters by high-performance liquid chromatography. Anal. Biochem. 153:45-49.
    • (1986) Anal. Biochem. , vol.153 , pp. 45-49
    • Hosokawa, Y.1    Shimomura, Y.2    Harris, R.A.3    Ozawa, T.4
  • 15
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid, E., C. Rappleye, I. Stojiljkovic, and J. Roth. 1999. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. J. Bacteriol. 181:5317-5329.
    • (1999) J. Bacteriol. , vol.181 , pp. 5317-5329
    • Kofoid, E.1    Rappleye, C.2    Stojiljkovic, I.3    Roth, J.4
  • 16
    • 0013894468 scopus 로고
    • The role and control of the glyoxylate cycle in Escherichia coli
    • Kornberg, H. L. 1966. The role and control of the glyoxylate cycle in Escherichia coli. Biochem. J. 99:1-11.
    • (1966) Biochem. J. , vol.99 , pp. 1-11
    • Kornberg, H.L.1
  • 18
    • 0029009026 scopus 로고
    • Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli
    • Kumari, S., R. Tishel, M. Eisenbach, and A. J. Wolfe. 1995. Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli. J. Bacteriol. 177:2878-2886.
    • (1995) J. Bacteriol. , vol.177 , pp. 2878-2886
    • Kumari, S.1    Tishel, R.2    Eisenbach, M.3    Wolfe, A.J.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage and structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage and structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0024962598 scopus 로고
    • Activation of acetate by Methanosarcina thermophila. Purification and characterization of phosphotransacetylase
    • Lundie, L. L., Jr., and J. G. Ferry. 1989. Activation of acetate by Methanosarcina thermophila. Purification and characterization of phosphotransacetylase. J. Biol. Chem. 264:18392-18396.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18392-18396
    • Lundie Jr., L.L.1    Ferry, J.G.2
  • 21
    • 0024075956 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium
    • Roof, D. M., and J. R. Roth. 1988. Ethanolamine utilization in Salmonella typhimurium. J. Bacteriol. 170:3855-3863.
    • (1988) J. Bacteriol. , vol.170 , pp. 3855-3863
    • Roof, D.M.1    Roth, J.R.2
  • 22
    • 0024393078 scopus 로고
    • 12-dependent ethanolamine utilization in Salmonella typhimurium
    • 12-dependent ethanolamine utilization in Salmonella typhimurium. J. Bacteriol. 171:3316-3323.
    • (1989) J. Bacteriol. , vol.171 , pp. 3316-3323
    • Roof, D.M.1    Roth, J.R.2
  • 23
    • 0001870287 scopus 로고
    • Detection of proteins
    • F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Wiley Interscience, New York, N.Y.
    • Sasse, J. 1991. Detection of proteins, p. 10.6.1-10.6.8. In F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley Interscience, New York, N.Y.
    • (1991) Current Protocols in Molecular Biology , vol.1 , pp. 1061-1068
    • Sasse, J.1
  • 24
    • 0042338528 scopus 로고    scopus 로고
    • Computational study on mechanistic details of the aminoethanol rearrangement catalyzed by the vitamin B(12)-dependent ethanolamine ammonia lyase: His and asp/glu acting simultaneously as catalytic auxiliaries
    • Semialjac, M., and H. Schwarz. 2003. Computational study on mechanistic details of the aminoethanol rearrangement catalyzed by the vitamin B(12)-dependent ethanolamine ammonia lyase: his and asp/glu acting simultaneously as catalytic auxiliaries. J. Org. Chem. 68:6967-6983.
    • (2003) J. Org. Chem. , vol.68 , pp. 6967-6983
    • Semialjac, M.1    Schwarz, H.2
  • 25
    • 0028944586 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutj eutH gene cluster
    • Stojiljkovic, I., A. J. Bäumler, and F. Heffron. 1995. Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutj eutH gene cluster. J. Bacteriol. 177:1357-1366.
    • (1995) J. Bacteriol. , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Bäumler, A.J.2    Heffron, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.