메뉴 건너뛰기




Volumn 125, Issue 2, 2000, Pages 205-210

Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii

Author keywords

Acetohydroxy acid synthase; Amino acid biosynthesis; Archaea; Branched chain amino acids; Euryarchaeota; Haloferax volcanii; Halophile

Indexed keywords

ACETOLACTATE SYNTHASE; BRANCHED CHAIN AMINO ACID; SODIUM CHLORIDE;

EID: 0034015689     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(99)00170-4     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0030029174 scopus 로고    scopus 로고
    • 3-hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: Purification, characterization, and expression in Escherichia coli
    • Bischoff, K.M., Rodwell, V.W., 1996. 3-hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: purification, characterization, and expression in Escherichia coli. J. Bacteriol. 178, 19-23.
    • (1996) J. Bacteriol. , vol.178 , pp. 19-23
    • Bischoff, K.M.1    Rodwell, V.W.2
  • 2
    • 0030940004 scopus 로고    scopus 로고
    • Cloning and phylogenetic analysis of the genes encoding acetohydroxyacid synthase from the archaeon Methanococcus aeolicus
    • Bowen, T.L., Union, J., Tumbula, D.L., Whitman, W.B., 1997. Cloning and phylogenetic analysis of the genes encoding acetohydroxyacid synthase from the archaeon Methanococcus aeolicus. Gene 188, 77-84.
    • (1997) Gene , vol.188 , pp. 77-84
    • Bowen, T.L.1    Union, J.2    Tumbula, D.L.3    Whitman, W.B.4
  • 4
    • 0028810373 scopus 로고
    • Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: Enzyme purification, characterisation and N-terminal sequence
    • Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J., Hough, D.W., 1995. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134, 85-90.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 85-90
    • Camacho, M.L.1    Brown, R.A.2    Bonete, M.J.3    Danson, M.J.4    Hough, D.W.5
  • 5
    • 0032537483 scopus 로고    scopus 로고
    • Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases
    • Chipman, D., Barak, Z., Schloss, J.V., 1998. Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Biochim. Biophys. Acta 1385, 401-419.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 401-419
    • Chipman, D.1    Barak, Z.2    Schloss, J.V.3
  • 6
    • 0021352116 scopus 로고
    • Purification and subunit composition of acetohydroxy acid synthase I from Escherichia coli
    • Eoyang, L., Silverman, P.M., 1984. Purification and subunit composition of acetohydroxy acid synthase I from Escherichia coli. J. Bacteriol. 157, 184-189.
    • (1984) J. Bacteriol. , vol.157 , pp. 184-189
    • Eoyang, L.1    Silverman, P.M.2
  • 7
    • 0022652882 scopus 로고
    • Role of small subunit (ilvN polypepetide) of acetohydroxy acid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition
    • Eoyang, L., Silverman, P.M., 1986. Role of small subunit (ilvN polypepetide) of acetohydroxy acid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition. J. Bacteriol. 166, 901-904.
    • (1986) J. Bacteriol. , vol.166 , pp. 901-904
    • Eoyang, L.1    Silverman, P.M.2
  • 8
    • 0031857516 scopus 로고    scopus 로고
    • Branched-chain amino acid biosynthesis in Salmonella typhimurium: A quantitative analysis
    • Epelbaum, S., LaRossa, R.A., Van Dyk, T.K., Elkayam, T., Chipman, D.M., Barak, Z., 1998. Branched-chain amino acid biosynthesis in Salmonella typhimurium: a quantitative analysis. J. Bacteriol. 180, 4056-4067.
    • (1998) J. Bacteriol. , vol.180 , pp. 4056-4067
    • Epelbaum, S.1    LaRossa, R.A.2    Van Dyk, T.K.3    Elkayam, T.4    Chipman, D.M.5    Barak, Z.6
  • 9
    • 0024208277 scopus 로고
    • Assay of products of acetolactate synthase
    • Gollop, N., Barak, Z., Chipman, D.M., 1988. Assay of products of acetolactate synthase. Methods Enzymol. 166, 234-240.
    • (1988) Methods Enzymol. , vol.166 , pp. 234-240
    • Gollop, N.1    Barak, Z.2    Chipman, D.M.3
  • 10
    • 0024323602 scopus 로고
    • Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli
    • Gollop, N., Damri, B., Barak, Z., Chipman, D.M., 1989. Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli. Biochemistry 28, 6310-6317.
    • (1989) Biochemistry , vol.28 , pp. 6310-6317
    • Gollop, N.1    Damri, B.2    Barak, Z.3    Chipman, D.M.4
  • 11
    • 0025346177 scopus 로고
    • Physiological implications of the substrate specificities of acetohydroxy acid synthases from various organisms
    • Gollop, N., Damri, B., Chipman, D.M., Barak, Z., 1990. Physiological implications of the substrate specificities of acetohydroxy acid synthases from various organisms. J. Bacteriol. 172, 3444-3449.
    • (1990) J. Bacteriol. , vol.172 , pp. 3444-3449
    • Gollop, N.1    Damri, B.2    Chipman, D.M.3    Barak, Z.4
  • 12
    • 21344477132 scopus 로고
    • Histidase activity of the halophilic archaebacterium, Haloferax volcanii
    • Kauri, T., Ahonkhai, I., Desjardins, M., Kushner, D.J., 1993. Histidase activity of the halophilic archaebacterium, Haloferax volcanii. Microbios 76, 245-249.
    • (1993) Microbios , vol.76 , pp. 245-249
    • Kauri, T.1    Ahonkhai, I.2    Desjardins, M.3    Kushner, D.J.4
  • 14
    • 0023096487 scopus 로고
    • Effects of deletion and insertion mutations in the ilvM gene of Escherichia coli
    • Lu, M.F., Umbarger, H.E., 1987. Effects of deletion and insertion mutations in the ilvM gene of Escherichia coli. J. Bacteriol. 169, 600-604.
    • (1987) J. Bacteriol. , vol.169 , pp. 600-604
    • Lu, M.F.1    Umbarger, H.E.2
  • 15
    • 0010704785 scopus 로고
    • + active transport in the archaebacterium Haloferax volcanii
    • + active transport in the archaebacterium Haloferax volcanii. Arch. Microbiol. 151, 530-536.
    • (1989) Arch. Microbiol. , vol.151 , pp. 530-536
    • Meury, J.1    Kohiyama, M.2
  • 16
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech, M., Werczberger, R., 1985. Genetic transfer in Halobacterium volcanii. J. Bacteriol. 162, 461-462.
    • (1985) J. Bacteriol. , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 17
    • 34250398425 scopus 로고
    • Halobacterium volcanii spec, nov., a Dead Sea halobacterium with a moderate salt requirement
    • Mullakhanbhai, M.F., Larsen, H., 1975. Halobacterium volcanii spec, nov., a Dead Sea halobacterium with a moderate salt requirement. Arch. Microbiol. 104, 207-214.
    • (1975) Arch. Microbiol. , vol.104 , pp. 207-214
    • Mullakhanbhai, M.F.1    Larsen, H.2
  • 18
    • 12944301235 scopus 로고
    • Characterization of the dominant halophilic archaea in a bacterial bloom in the Dead Sea
    • Oren, A., Gurevich, P., 1995. Characterization of the dominant halophilic archaea in a bacterial bloom in the Dead Sea. FEMS Microbiol. Ecol. 14, 147-156.
    • (1995) FEMS Microbiol. Ecol. , vol.14 , pp. 147-156
    • Oren, A.1    Gurevich, P.2
  • 19
    • 0022356249 scopus 로고
    • Purification and properties of Salmonella typhimurium aceltolactate synthase isozyme II form Escherichia coli HB101/pDU9
    • Schloss, J.V., Van Dyk, D.E., Vasta, J.F., Kutny, R.M., 1985. Purification and properties of Salmonella typhimurium aceltolactate synthase isozyme II form Escherichia coli HB101/pDU9. Biochemistry 24, 4952-4959.
    • (1985) Biochemistry , vol.24 , pp. 4952-4959
    • Schloss, J.V.1    Van Dyk, D.E.2    Vasta, J.F.3    Kutny, R.M.4
  • 20
    • 0031688651 scopus 로고    scopus 로고
    • Operation of glyoxylate cycle in halophilic archaea: Presence of malate synthase and isocitrate lyase in Haloferax volcanii
    • Serrano, J.A., Camacho, M., Bonete, M.J., 1998. Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii. FEBS Lett. 434, 13-16.
    • (1998) FEBS Lett. , vol.434 , pp. 13-16
    • Serrano, J.A.1    Camacho, M.2    Bonete, M.J.3
  • 22
    • 0001348712 scopus 로고    scopus 로고
    • Biosynthesis of the branched-chain amino acids
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., Umbarger, H. (Eds.), American Society for Microbiology, Washington, DC
    • Umbarger, H.E., 1996. Biosynthesis of the branched-chain amino acids. In: Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., Umbarger, H. (Eds.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, DC, pp. 442-457.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 442-457
    • Umbarger, H.E.1
  • 23
    • 0029798076 scopus 로고    scopus 로고
    • Isolation and charactherization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme
    • Vyazmensky, M., Sella, C., Barak, Z., Chipman, D.M., 1996. Isolation and charactherization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Biochemistry 35, 10339-10346.
    • (1996) Biochemistry , vol.35 , pp. 10339-10346
    • Vyazmensky, M.1    Sella, C.2    Barak, Z.3    Chipman, D.M.4
  • 24
    • 0026804680 scopus 로고
    • Properties of subcloned subunits of bacterial acetohydroxy acid synthases
    • Weinstock, O., Sella, C., Chipman, D.M., Barak, Z., 1992. Properties of subcloned subunits of bacterial acetohydroxy acid synthases. J. Bacteriol. 174, 5560-5566.
    • (1992) J. Bacteriol. , vol.174 , pp. 5560-5566
    • Weinstock, O.1    Sella, C.2    Chipman, D.M.3    Barak, Z.4
  • 25
    • 84864301531 scopus 로고
    • A colorimetric determination of blood acetoin
    • Westerfeld, W.W., 1945. A colorimetric determination of blood acetoin. J. Biol. Chem. 161, 495-502.
    • (1945) J. Biol. Chem. , vol.161 , pp. 495-502
    • Westerfeld, W.W.1
  • 26
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains archaea, bacteria and eucarya
    • Woese, C.R., Kandler, O., Wheelis, M.L., 1990. Towards a natural system of organisms: proposal for the domains archaea, bacteria and eucarya. Proc. Natl. Acad. Sci. USA 87, 4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 27
    • 0026032524 scopus 로고
    • Characterization of enzymes of the branched-chain amino acid biosynthesis pathway in Methanococcus spp.
    • Xing, R., Whitman, W.B., 1991. Characterization of enzymes of the branched-chain amino acid biosynthesis pathway in Methanococcus spp. J. Bacteriol. 173, 2086-2092.
    • (1991) J. Bacteriol. , vol.173 , pp. 2086-2092
    • Xing, R.1    Whitman, W.B.2
  • 28
    • 0028324793 scopus 로고
    • Purification and characterization of the oxygen-sensitive acetohydroxy acid synthase from the archaebacterium Methanococcus aeolicus
    • Xing, R., Whitman, W.B., 1994. Purification and characterization of the oxygen-sensitive acetohydroxy acid synthase from the archaebacterium Methanococcus aeolicus. J. Bacteriol. 176, 1207-1213.
    • (1994) J. Bacteriol. , vol.176 , pp. 1207-1213
    • Xing, R.1    Whitman, W.B.2
  • 29
    • 0024971668 scopus 로고
    • Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii
    • Zusman, T., Rosenshine, L, Boehm, G., Jaenicke, R., Leskiw, B., Mevarech, M., 1989. Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. J. Biol. Chem. 264, 18878-18883.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18878-18883
    • Zusman, T.1    Rosenshine, L.2    Boehm, G.3    Jaenicke, R.4    Leskiw, B.5    Mevarech, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.