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Volumn 179, Issue 24, 1997, Pages 7712-7717

Identification of cysteine and arginine residues essential for the phosphotransacetylase from Methanosarcina thermophila

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; BACTERIAL ENZYME; COENZYME A; CYSTEINE; GLUTAMINE; N ETHYLMALEIMIDE; PHOSPHATE ACETYLTRANSFERASE; SERINE;

EID: 0030779393     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.24.7712-7717.1997     Document Type: Article
Times cited : (21)

References (25)
  • 2
    • 0029762151 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of genes encoding phosphotransacetylase and acetate kinase from Clostridium acetobutylicum ATCC 824
    • Boynton, Z. L., G. N. Bennett, and F. B. Rudolph. 1996. Cloning, sequencing, and expression of genes encoding phosphotransacetylase and acetate kinase from Clostridium acetobutylicum ATCC 824. Appl. Environ. Microbiol. 62: 2758-2766.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2758-2766
    • Boynton, Z.L.1    Bennett, G.N.2    Rudolph, F.B.3
  • 3
    • 0026652496 scopus 로고
    • Effect of group-selective modification reagents on arylamine N-acetyltransferase activities
    • Cheon, H. G., and P. E. Hanna. 1992. Effect of group-selective modification reagents on arylamine N-acetyltransferase activities. Biochem. Pharmacol. 43:2255-2268.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2255-2268
    • Cheon, H.G.1    Hanna, P.E.2
  • 6
    • 0028674882 scopus 로고
    • Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus
    • Gupta, R. S., and B. Singh. 1994. Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus. Curr. Biol. 4:1104-1114.
    • (1994) Curr. Biol. , vol.4 , pp. 1104-1114
    • Gupta, R.S.1    Singh, B.2
  • 7
    • 0017064940 scopus 로고
    • Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase
    • Henkin, J., and R. H. Abeles. 1976. Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase. Biochemistry 15:3472-3479.
    • (1976) Biochemistry , vol.15 , pp. 3472-3479
    • Henkin, J.1    Abeles, R.H.2
  • 8
    • 0028138812 scopus 로고
    • Molecular cloning of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon, sequencing of the pta gene, and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli
    • Kakuda, H., K. Hosono, K. Shiroishi, and S. Ichihara. 1994. Molecular cloning of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon, sequencing of the pta gene, and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli. J. Biochem. 116: 916-922.
    • (1994) J. Biochem. , vol.116 , pp. 916-922
    • Kakuda, H.1    Hosono, K.2    Shiroishi, K.3    Ichihara, S.4
  • 9
    • 0028893719 scopus 로고
    • 634 for inhibition by maleimides but not catalysis
    • 634 for inhibition by maleimides but not catalysis. J. Biol. Chem. 270:2630-2635.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2630-2635
    • Kim, E.J.1    Zhen, R.2    Rea, P.A.3
  • 10
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 11
    • 0027382864 scopus 로고
    • Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila
    • Latimer, M. T., and J. G. Ferry. 1993. Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila. J. Bacteriol. 175:6822-6829.
    • (1993) J. Bacteriol. , vol.175 , pp. 6822-6829
    • Latimer, M.T.1    Ferry, J.G.2
  • 12
    • 0024962598 scopus 로고
    • Activation of acetate by Methanosarcina thermophila: Purification and characterization of phosphotransacetylase
    • Lundie, L. L., 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, L.L.1    Ferry, J.G.2
  • 14
    • 0030058857 scopus 로고    scopus 로고
    • Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila
    • Maupin-Furlow, J. A., and J. G. Ferry. 1996. Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. J. Bacteriol. 178:340-346.
    • (1996) J. Bacteriol. , vol.178 , pp. 340-346
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 15
    • 0029832099 scopus 로고    scopus 로고
    • Analysis of the CO dehydrogenase/acetyl-CoA synthase operon of Methanosarcina thermophila
    • Maupin-Furlow, J. A., and J. G. Ferry. 1996. Analysis of the CO dehydrogenase/acetyl-CoA synthase operon of Methanosarcina thermophila. J. Bacteriol. 178:6849-6856.
    • (1996) J. Bacteriol. , vol.178 , pp. 6849-6856
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 16
    • 0029853148 scopus 로고    scopus 로고
    • WWW-Query: An on-line retrieval system for biological sequence banks
    • Perrière, G., and M. Gouy. 1996. WWW-Query: an on-line retrieval system for biological sequence banks. Biochimie 78:364-369.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 17
    • 0027328367 scopus 로고
    • Phylogenetic analysis of anaerobic thermophilic bacteria: Aid for their reclassification
    • Rainey, F. A., N. L. Ward, H. W. Morgan, R. Toalster, and E. Stackebrandt. 1993. Phylogenetic analysis of anaerobic thermophilic bacteria: aid for their reclassification. J. Bacteriol. 175:4772-4779.
    • (1993) J. Bacteriol. , vol.175 , pp. 4772-4779
    • Rainey, F.A.1    Ward, N.L.2    Morgan, H.W.3    Toalster, R.4    Stackebrandt, E.5
  • 18
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution
    • Remington, S., G. Wiegand, and R. Huber. 1982. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158:111-152.
    • (1982) J. Mol. Biol. , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 20
    • 0025900043 scopus 로고
    • Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis
    • Schröder, I., R. P. Gunsalus, B. A. C. Ackrell, B. Cochran, and G. Cecchini. 1991. Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266:13572-13579.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13572-13579
    • Schröder, I.1    Gunsalus, R.P.2    Ackrell, B.A.C.3    Cochran, B.4    Cecchini, G.5
  • 21
    • 0024976544 scopus 로고
    • Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum
    • Shanmugasundaram, T., G. K. Kumar, B. C. Shenoy, and H. G. Wood. 1989. Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum. Biochemistry 28: 7112-7116.
    • (1989) Biochemistry , vol.28 , pp. 7112-7116
    • Shanmugasundaram, T.1    Kumar, G.K.2    Shenoy, B.C.3    Wood, H.G.4
  • 23
    • 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, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0028030937 scopus 로고
    • Identification of the reactive cysteine in clostridial glutamate dehydrogenase by site-directed mutagenesis and proof that this residue is not strictly essential
    • Wang, X., and P. C. Engel. 1994. Identification of the reactive cysteine in clostridial glutamate dehydrogenase by site-directed mutagenesis and proof that this residue is not strictly essential. Protein Eng. 7:1013-1016.
    • (1994) Protein Eng. , vol.7 , pp. 1013-1016
    • Wang, X.1    Engel, P.C.2
  • 25
    • 0019480175 scopus 로고
    • Evidence for an essential arginine residue at the active site of Escherichia coli acetate kinase
    • Wong, S. S., and L. C. Wong. 1981. Evidence for an essential arginine residue at the active site of Escherichia coli acetate kinase. Biochim. Biophys. Acta 660:142-147.
    • (1981) Biochim. Biophys. Acta , vol.660 , pp. 142-147
    • Wong, S.S.1    Wong, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.