메뉴 건너뛰기




Volumn 69, Issue 7, 2003, Pages 3849-3857

Characterization and molecular cloning of a novel enzyme, inorganic polyphosphate/ATP-glucomannokinase, of Arthrobacter sp. strain KM

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CLONING; DNA SEQUENCES; GENETIC ENGINEERING; GLUCOSE; MOLECULAR DYNAMICS; MONOMERS;

EID: 0038493612     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.7.3849-3857.2003     Document Type: Article
Times cited : (39)

References (29)
  • 2
    • 0025663414 scopus 로고
    • Sequence and genetic organization of Zymomonas mobilis gene cluster that encodes several enzymes of glucose metabolism
    • Barnell, W. O., K. C. Yi, and T. Conway. 1990. Sequence and genetic organization of Zymomonas mobilis gene cluster that encodes several enzymes of glucose metabolism. J. Bacteriol. 172:7227-7240.
    • (1990) J. Bacteriol. , vol.172 , pp. 7227-7240
    • Barnell, W.O.1    Yi, K.C.2    Conway, T.3
  • 3
    • 0026012342 scopus 로고
    • Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A
    • Bonting, C. F. C., G. J. J. Kortstee, and A. J. B. Zehnder. 1991. Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A. J. Bacteriol. 173:6484-6488.
    • (1991) J. Bacteriol. , vol.173 , pp. 6484-6488
    • Bonting, C.F.C.1    Kortstee, G.J.J.2    Zehnder, A.J.B.3
  • 4
    • 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. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0027518532 scopus 로고
    • The competition plot: A simple test of whether two reactions occur at the same active site
    • Chevillard, C., M. L. Cardenas, and A. Cornish-bowden. 1993. The competition plot: a simple test of whether two reactions occur at the same active site. Biochem. J. 289:599-604.
    • (1993) Biochem. J. , vol.289 , pp. 599-604
    • Chevillard, C.1    Cardenas, M.L.2    Cornish-Bowden, A.3
  • 6
    • 0023109255 scopus 로고
    • Preparation of standards and determination of sizes of long-chain polyphosphates by gel electrophoresis
    • Clark, J. E., and H. G. Wood. 1987. Preparation of standards and determination of sizes of long-chain polyphosphates by gel electrophoresis. Anal. Biochem. 161:280-290.
    • (1987) Anal. Biochem. , vol.161 , pp. 280-290
    • Clark, J.E.1    Wood, H.G.2
  • 7
    • 0037604551 scopus 로고
    • Enzymes
    • E. E. Conn, P. K. Stumpe, G. Bruening, and R. H. Doi (ed.). John Wiley and Sons, New York, N.Y.
    • Conn, E. E., P. K. Stumpe., G. Bruening., and R. H. Doi. 1987. Enzymes, p. 115-163. In E. E. Conn, P. K. Stumpe, G. Bruening, and R. H. Doi (ed.), Outlines of biochemistry. John Wiley and Sons, New York, N.Y.
    • (1987) Outlines of Biochemistry , pp. 115-163
    • Conn, E.E.1    Stumpe, P.K.2    Bruening, G.3    Doi, R.H.4
  • 8
    • 0035047007 scopus 로고    scopus 로고
    • 14 and its potential role in regulating β-glucanase expression
    • 14 and its potential role in regulating β-glucanase expression. Microbiology 147:1035-1043.
    • (2001) Microbiology , vol.147 , pp. 1035-1043
    • Fields, M.W.1    Russell, J.B.2
  • 9
    • 0027546956 scopus 로고
    • Purification of polyphosphate and ATP glucose phosphotransferase from Mycobacterium tuberculosis H37Ra: Evidence that poly(P) and ATP glucokinase activities are catalyzed by the same enzyme
    • Hsieh, P. C., B. C. Shenoy, J. E. Jentoft, and N. F. B. Phillips. 1993. Purification of polyphosphate and ATP glucose phosphotransferase from Mycobacterium tuberculosis H37Ra: evidence that poly(P) and ATP glucokinase activities are catalyzed by the same enzyme. Protein Expr. Purif. 4:76-84.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 76-84
    • Hsieh, P.C.1    Shenoy, B.C.2    Jentoft, J.E.3    Phillips, N.F.B.4
  • 10
    • 0030003499 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of polyphosphate glucokinase from Mycobacterium tuberculosis
    • Hsieh, P. C., B. C. Shenoy, D. Samols, and N. F. B. Phillips. 1996. Cloning, expression, and characterization of polyphosphate glucokinase from Mycobacterium tuberculosis. J. Biol. Chem. 271:4909-4915.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4909-4915
    • Hsieh, P.C.1    Shenoy, B.C.2    Samols, D.3    Phillips, N.F.B.4
  • 11
    • 0000608931 scopus 로고
    • Adenosine 5′-diphosphate and adenosine 5′-monophosphate
    • H. U. Bergmeyer, J. Bergmeyer, and M. Graßl (ed.). Verlagsgesellschaft mbH, Weinheim, Germany
    • Jaworek, D., and J. Welsch. 1985. Adenosine 5′-diphosphate and adenosine 5′-monophosphate, p. 365-370. In H. U. Bergmeyer, J. Bergmeyer, and M. Graßl (ed.), Methods of enzymatic analysis, vol. 7. Verlagsgesellschaft mbH, Weinheim, Germany.
    • (1985) Methods of Enzymatic Analysis , vol.7 , pp. 365-370
    • Jaworek, D.1    Welsch, J.2
  • 13
    • 0032601578 scopus 로고    scopus 로고
    • Inorganic polyphosphate: A molecule of many functions
    • H. C. Schröder and W. E. G. Müller (ed.). Springer-Verlag, New York, N.Y.
    • Kornberg, A. 1999. Inorganic polyphosphate: a molecule of many functions, p. 1-16. In H. C. Schröder and W. E. G. Müller (ed.), Inorganic polyphosphates, vol. 23. Springer-Verlag, New York, N.Y.
    • (1999) Inorganic Polyphosphates , vol.23 , pp. 1-16
    • Kornberg, A.1
  • 14
    • 0015035928 scopus 로고
    • The detection of a new enzyme, 1,3-phosphoglycerate-polyphosphate phosphotransferase, in Neurospora crassa
    • Kulaev, I. S., and M. A. Bobyk. 1971. The detection of a new enzyme, 1,3-phosphoglycerate-polyphosphate phosphotransferase, in Neurospora crassa. Biokhimiya 36:426-429.
    • (1971) Biokhimiya , vol.36 , pp. 426-429
    • Kulaev, I.S.1    Bobyk, M.A.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of 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
  • 16
    • 17144464667 scopus 로고    scopus 로고
    • Cloning, functional expression and partial characterization of the glucose kinase from Renibacterium salmoninarum
    • Margarita, I. C., and L. Gloria. 2000. Cloning, functional expression and partial characterization of the glucose kinase from Renibacterium salmoninarum. FEMS Microbiol. Lett. 186:97-101.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 97-101
    • Margarita, I.C.1    Gloria, L.2
  • 17
    • 0038618743 scopus 로고
    • Properties of polyphosphate glucokinase in Acromobacter butyri
    • Murata, K., J. Kato, and I. Chibata. 1978. Properties of polyphosphate glucokinase in Acromobacter butyri. Agric. Biol. Chem. 42:2221-2226.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2221-2226
    • Murata, K.1    Kato, J.2    Chibata, I.3
  • 18
  • 19
    • 0023008879 scopus 로고
    • Polyphosphate glucokinase from Propionibacterium shermanii
    • Pepin, C. A., and H. G. Wood. 1986. Polyphosphate glucokinase from Propionibacterium shermanii. J. Biol. Chem. 261:4476-4480.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4476-4480
    • Pepin, C.A.1    Wood, H.G.2
  • 20
    • 0027293592 scopus 로고
    • The polyphosphate and ATP-dependent glucokinase from Propionibacterium shermanii: Both activities are catalyzed by the same protein
    • Phillip, N. F. B., P. J. Horn, and H. G. Wood. 1993. The polyphosphate and ATP-dependent glucokinase from Propionibacterium shermanii: both activities are catalyzed by the same protein. Arch. Biochem. Biophys. 300:309-319.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 309-319
    • Phillip, N.F.B.1    Horn, P.J.2    Wood, H.G.3
  • 21
    • 0037604535 scopus 로고    scopus 로고
    • Polyphosphate glucokinase
    • H. C. Schröder and W. E. G. Müller (ed.). Springer-Verlag, New York, N.Y.
    • Phillip, N. F. B., P. C. Hsieh, and T. H, Kowalczyk. 1999. Polyphosphate glucokinase, p. 101-122. In H. C. Schröder and W. E. G. Müller (ed.), Inorganic polyphosphates, vol. 23. Springer-Verlag, New York, N.Y.
    • (1999) Inorganic Polyphosphates , vol.23 , pp. 101-122
    • Phillip, N.F.B.1    Hsieh, P.C.2    Kowalczyk, T.H.3
  • 22
    • 0031782381 scopus 로고    scopus 로고
    • The glucose kinase of Bacillus subtilis
    • Pierre, S., and D. Michael. 1998. The glucose kinase of Bacillus subtilis. J. Bacteriol. 180:3222-3226.
    • (1998) J. Bacteriol. , vol.180 , pp. 3222-3226
    • Pierre, S.1    Michael, D.2
  • 23
    • 0015504296 scopus 로고
    • Identification and properties of an inducible mannokinase from Streptomyces violaceoruber
    • Sabater, B., J. Sebastian, and C. Asensio. 1972. Identification and properties of an inducible mannokinase from Streptomyces violaceoruber. Biochim. Biophys. Acta 284:406-413.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 406-413
    • Sabater, B.1    Sebastian, J.2    Asensio, C.3
  • 24
    • 0014199266 scopus 로고
    • An adenosine 5′-triphosphate: Hexose-6-phosphotransferase specific for D-mannose and D-fructose from Leuconostoc mesenteroides
    • Sapico, V., and R. L. Anderson. 1967. An adenosine 5′-triphosphate:hexose-6-phosphotransferase specific for D-mannose and D-fructose from Leuconostoc mesenteroides. J. Biol. Chem. 242:5086-5091.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5086-5091
    • Sapico, V.1    Anderson, R.L.2
  • 25
    • 0014213175 scopus 로고
    • Identification of a mannokinase in Escherichia coli
    • , Sebastian, J., and C. Asenosio. 1967. Identification of a mannokinase in Escherichia coli. Biochem. Biophys. Res. Commun. 28:197-202.
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 197-202
    • Sebastian, J.1    Asenosio, C.2
  • 26
    • 0034662398 scopus 로고    scopus 로고
    • Characterization of glk coding for glucose kinase of Corynebacterium glutamicum
    • Sun, Y. P., K. K. Hyung, K. Y. Seung, K. O. Tae, and K. L. Jung. 2000. Characterization of glk coding for glucose kinase of Corynebacterium glutamicum. FEMS Microbiol. Lett. 188:209-215.
    • (2000) FEMS Microbiol. Lett. , vol.188 , pp. 209-215
    • Sun, Y.P.1    Hyung, K.K.2    Seung, K.Y.3    Tae, K.O.4    Jung, K.L.5
  • 27
    • 0000183334 scopus 로고
    • Inorganic polyphosphate glucokinase of Mycobacterium phlei
    • Szymona, M., and W. Ostrowski. 1964. Inorganic polyphosphate glucokinase of Mycobacterium phlei. Biochim. Biophys. Acta 85:283-295.
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 283-295
    • Szymona, M.1    Ostrowski, W.2
  • 28
    • 4243284293 scopus 로고
    • Phosphorylation of nucleosides with polyphosphoric acid
    • Waehneldt, T. V., and S. Fox. 1967. Phosphorylation of nucleosides with polyphosphoric acid. Biochim. Biophys. Acta 134:9-16.
    • (1967) Biochim. Biophys. Acta , vol.134 , pp. 9-16
    • Waehneldt, T.V.1    Fox, S.2
  • 29
    • 0026358279 scopus 로고
    • Volcanic production of polyphosphates and its relevance to prebiotic evolution
    • Yamagata, Y., H. Watanabe, M. Saitoh, and T. Namba. 1991. Volcanic production of polyphosphates and its relevance to prebiotic evolution. Nature 352:516-519.
    • (1991) Nature , vol.352 , pp. 516-519
    • Yamagata, Y.1    Watanabe, H.2    Saitoh, M.3    Namba, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.