메뉴 건너뛰기




Volumn 61, Issue 16, 2004, Pages 2020-2030

Acetyl-coenzyme A synthetase (AMP forming)

Author keywords

Acetate; Acetyl coenzyme A; Chromosome stability; CoA ligase; Gene expression; Gene silencing; Lifespan; Sirtuins; Two carbon metabolism

Indexed keywords

ACETIC ACID; ACETYL COENZYME A; ACETYL COENZYME A SYNTHETASE; CARBON; NICOTINAMIDE ADENINE DINUCLEOTIDE; SIRTUIN;

EID: 4344570067     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-3448-x     Document Type: Review
Times cited : (186)

References (106)
  • 1
    • 0001869573 scopus 로고    scopus 로고
    • Anaerobic energy generation
    • Lengler J. W., Drews G. and Chlegel H. G. (eds) Thieme, Stuttgart
    • Buckel W. (1999) Anaerobic energy generation, In: Biology of the Procaryotes, pp. 278-326, (Lengler J. W., Drews G. and Chlegel H. G. (eds) Thieme, Stuttgart
    • (1999) Biology of the Procaryotes , pp. 278-326
    • Buckel, W.1
  • 2
    • 0023276469 scopus 로고
    • Short chain fatty acids in human large intestine, portal, hepatic and venous blood
    • Cummings J. H., Pomare E. W., Branch W. J., Naylor C. P. and Macfarlane G. T. (1987) Short chain fatty acids in human large intestine, portal, hepatic and venous blood. Gut 28: 1221-1227
    • (1987) Gut , vol.28 , pp. 1221-1227
    • Cummings, J.H.1    Pomare, E.W.2    Branch, W.J.3    Naylor, C.P.4    Macfarlane, G.T.5
  • 4
    • 0017759929 scopus 로고
    • The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli
    • Brown T. D., Jones-Mortimer M. C. and Kornberg H. L. (1977) The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J. Gen. Microbiol. 102: 327-336
    • (1977) J. Gen. Microbiol. , vol.102 , pp. 327-336
    • Brown, T.D.1    Jones-Mortimer, M.C.2    Kornberg, H.L.3
  • 5
    • 0035158122 scopus 로고    scopus 로고
    • Urkinase: Structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases
    • Buss K. A., Cooper D. R., Ingram-Smith C., Ferry J. G., Sanders D. A. and Hasson M. S. (2001) Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183: 680-686
    • (2001) J. Bacteriol. , vol.183 , pp. 680-686
    • Buss, K.A.1    Cooper, D.R.2    Ingram-Smith, C.3    Ferry, J.G.4    Sanders, D.A.5    Hasson, M.S.6
  • 7
    • 0027207516 scopus 로고
    • Is acetyl phosphate a global signal in Escherichia coli?
    • McCleary W. R., Stock J. B. and Ninfa A. J. (1993) Is acetyl phosphate a global signal in Escherichia coli? J. Bacteriol. 175: 2793-2798
    • (1993) J. Bacteriol. , vol.175 , pp. 2793-2798
    • McCleary, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 8
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary W. R. and Stock J. B. (1994) Acetyl phosphate and the activation of two-component response regulators. J. Biol. Chem. 269: 31567-31572
    • (1994) J. Biol. Chem. , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 9
    • 0034195202 scopus 로고    scopus 로고
    • From 'reactive C2 units' to acetyl coenzyme A: A long trail with an acetyl phosphate detour
    • Bentley R. (2000) From 'reactive C2 units' to acetyl coenzyme A: a long trail with an acetyl phosphate detour. Trends Biochem. Sci. 25: 302-305
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 302-305
    • Bentley, R.1
  • 11
    • 0026560385 scopus 로고
    • Involvement of phosphotransacetylase, acetate kinase and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli
    • Wanner B. L. and Wilmes-Riesenberg M. R. (1992) Involvement of phosphotransacetylase, acetate kinase and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli. J. Bacteriol. 174: 2124-2130
    • (1992) J. Bacteriol. , vol.174 , pp. 2124-2130
    • Wanner, B.L.1    Wilmes-Riesenberg, M.R.2
  • 12
    • 0017615796 scopus 로고
    • An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase
    • Reeves R. E., Warren L. G., Susskind B. and Lo H. S. (1977) An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase. J. Biol. Chem. 252: 726-731
    • (1977) J. Biol. Chem. , vol.252 , pp. 726-731
    • Reeves, R.E.1    Warren, L.G.2    Susskind, B.3    Lo, H.S.4
  • 13
    • 0018995165 scopus 로고
    • Energy metabolism of the anaerobic protozoon Giardia lamblia
    • Lindmark D. G. (1980) Energy metabolism of the anaerobic protozoon Giardia lamblia. Mol. Biochem. Parasitol. 1: 1-12
    • (1980) Mol. Biochem. Parasitol. , vol.1 , pp. 1-12
    • Lindmark, D.G.1
  • 14
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • Muller M. (1988) Energy metabolism of protozoa without mitochondria. Annu. Rev. Microbiol. 42: 465-488
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 465-488
    • Muller, M.1
  • 15
    • 0026083153 scopus 로고
    • Pyruvate metabolism of the hyperthermophilic archaebacterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalyzed by an acetyl-CoA synthetase (ADP-forming)
    • Schäfer T. and Schönheit P. (1991) Pyruvate metabolism of the hyperthermophilic archaebacterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalyzed by an acetyl-CoA synthetase (ADP-forming). Arch. Microbiol. 155: 366-377
    • (1991) Arch. Microbiol. , vol.155 , pp. 366-377
    • Schäfer, T.1    Schönheit, P.2
  • 16
    • 0031039802 scopus 로고    scopus 로고
    • Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
    • Glasemacher J., Bock A. K., Schmid R. and Schönheit P. (1997) Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 244: 561-567
    • (1997) Eur. J. Biochem. , vol.244 , pp. 561-567
    • Glasemacher, J.1    Bock, A.K.2    Schmid, R.3    Schönheit, P.4
  • 17
    • 0033614003 scopus 로고    scopus 로고
    • A detailed structural description of Escherichia coli succinyl-CoA synthetase
    • Fraser M. E., James M. N., Bridger W. A. and Wolodko W. T. (1999) A detailed structural description of Escherichia coli succinyl-CoA synthetase. J. Mol. Biol. 285: 1633-1653
    • (1999) J. Mol. Biol. , vol.285 , pp. 1633-1653
    • Fraser, M.E.1    James, M.N.2    Bridger, W.A.3    Wolodko, W.T.4
  • 18
    • 0034635193 scopus 로고    scopus 로고
    • ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography
    • Joyce M. A., Fraser M. E., James M. N., Bridger W. A. and Wolodko W. T. (2000) ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography. Biochemistry 39: 17-25
    • (2000) Biochemistry , vol.39 , pp. 17-25
    • Joyce, M.A.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4    Wolodko, W.T.5
  • 19
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel M. A., Stachelhaus T. and Mootz H. D. (1997) Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97: 2651-2674
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 20
    • 0037453033 scopus 로고    scopus 로고
    • Polyketide and non-ribosomal peptide synthases: Falling together by coming apart
    • Hutchinson C. R. (2003) Polyketide and non-ribosomal peptide synthases: falling together by coming apart. Proc. Natl. Acad. Sci. USA 100: 3010-3012
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3010-3012
    • Hutchinson, C.R.1
  • 22
    • 0035831486 scopus 로고    scopus 로고
    • The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
    • May J. J., Wendrich T. M. and Marahiel M. A. (2001) The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276: 7209-7217
    • (2001) J. Biol. Chem. , vol.276 , pp. 7209-7217
    • May, J.J.1    Wendrich, T.M.2    Marahiel, M.A.3
  • 23
    • 0036825397 scopus 로고    scopus 로고
    • Purification and partial characterization of acetyl-coA synthetase in rat liver mitochondria
    • Tokyo
    • Yamashita H., Fukuura A., Nakamura T., Kaneyuki T., Kimoto M. and Hiemori M. et al. (2002) Purification and partial characterization of acetyl-coA synthetase in rat liver mitochondria. J. Nutr. Sci. Vitaminol. (Tokyo) 48: 359-364
    • (2002) J. Nutr. Sci. Vitaminol. , vol.48 , pp. 359-364
    • Yamashita, H.1    Fukuura, A.2    Nakamura, T.3    Kaneyuki, T.4    Kimoto, M.5    Hiemori, M.6
  • 24
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • Fujino T., Kondo J., Ishikawa M., Morikawa K. and Yamamoto T. T. (2001) Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J. Biol. Chem. 276: 11420-11426
    • (2001) J. Biol. Chem. , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 25
    • 0029134555 scopus 로고
    • ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose
    • Van den Berg M. A. and Steensma H. Y. (1995) ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose. Eur. J. Biochem. 231: 704-713
    • (1995) Eur. J. Biochem. , vol.231 , pp. 704-713
    • Van Den Berg, M.A.1    Steensma, H.Y.2
  • 26
    • 0027062806 scopus 로고
    • Cloning and disruption of a gene required for growth on acetate but not on ethanol: The acetylcoenzyme A synthetase gene of Saccharomyces cerevisiae
    • De Virgilio C., Burckert N., Barth G., Neuhaus J. M., Boller T. and Wiemken A. (1992) Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetylcoenzyme A synthetase gene of Saccharomyces cerevisiae. Yeast 8: 1043-1051
    • (1992) Yeast , vol.8 , pp. 1043-1051
    • De Virgilio, C.1    Burckert, N.2    Barth, G.3    Neuhaus, J.M.4    Boller, T.5    Wiemken, A.6
  • 27
    • 0036273555 scopus 로고    scopus 로고
    • Expression of cytosolic acetyl-CoA synthetase gene is developmentally regulated
    • Loikkanen I., Haghighi S., Vainio S. and Pajunen A. (2002) Expression of cytosolic acetyl-CoA synthetase gene is developmentally regulated. Mech. Dev. 115: 139-141
    • (2002) Mech. Dev. , vol.115 , pp. 139-141
    • Loikkanen, I.1    Haghighi, S.2    Vainio, S.3    Pajunen, A.4
  • 28
    • 0035823629 scopus 로고    scopus 로고
    • Transcriptional regulation of the murine acetyl-CoA synthetase 1 gene through multiple clustered binding sites for sterol regulatory element-binding proteins and a single neighboring site for Sp1
    • Ikeda Y., Yamamoto J., Okamura M., Fujino T., Takahashi S. and Takenshi K. et al. (2001) Transcriptional regulation of the murine acetyl-CoA synthetase 1 gene through multiple clustered binding sites for sterol regulatory element-binding proteins and a single neighboring site for Sp1. J. Biol. Chem. 276: 34259-34269
    • (2001) J. Biol. Chem. , vol.276 , pp. 34259-34269
    • Ikeda, Y.1    Yamamoto, J.2    Okamura, M.3    Fujino, T.4    Takahashi, S.5    Takenshi, K.6
  • 29
    • 0022988305 scopus 로고
    • Acetate metabolism by tissues of the rabbit
    • Woodnutt G. and Parker D. S. (1986) Acetate metabolism by tissues of the rabbit. Comp. Biochem. Physiol. B 85: 487-490
    • (1986) Comp. Biochem. Physiol. B , vol.85 , pp. 487-490
    • Woodnutt, G.1    Parker, D.S.2
  • 30
    • 0025738416 scopus 로고
    • Isolation and characterization of carnitine acetyltransferase from S. cerevisiae
    • Kispal G., Cseko J., Alkonyi I. and Sandor A. (1991) Isolation and characterization of carnitine acetyltransferase from S. cerevisiae. Biochim. Biophys. Acta 1085: 217-222
    • (1991) Biochim. Biophys. Acta , vol.1085 , pp. 217-222
    • Kispal, G.1    Cseko, J.2    Alkonyi, I.3    Sandor, A.4
  • 31
    • 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
  • 32
    • 0025008687 scopus 로고
    • Hibernation activates glyoxylate cycle and gluconeogenesis in black bear brown adipose tissue
    • Davis W. L., Goodman D. B., Crawford L. A., Cooper O. J. and Matthews J. L. (1990) Hibernation activates glyoxylate cycle and gluconeogenesis in black bear brown adipose tissue. Biochim. Biophys. Acta 1051: 276-278
    • (1990) Biochim. Biophys. Acta , vol.1051 , pp. 276-278
    • Davis, W.L.1    Goodman, D.B.2    Crawford, L.A.3    Cooper, O.J.4    Matthews, J.L.5
  • 33
    • 0035819933 scopus 로고    scopus 로고
    • Molecular evolution of the AMP-forming acetyl-CoA synthetase
    • Karan D., David J. R. and Capy P. (2001) Molecular evolution of the AMP-forming acetyl-CoA synthetase. Gene 265: 95-101
    • (2001) Gene , vol.265 , pp. 95-101
    • Karan, D.1    David, J.R.2    Capy, P.3
  • 34
    • 0001640692 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction: Isolation and characterization of enzyme-bound acetyl adenylate
    • Webster J., L. T. (1963) Studies of the acetyl coenzyme A synthetase reaction: Isolation and characterization of enzyme-bound acetyl adenylate. J. Biol. Chem. 238: 4010-4015
    • (1963) J. Biol. Chem. , vol.238 , pp. 4010-4015
    • Webster Jr., L.T.1
  • 35
    • 0013814145 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase
    • Webster L. T. Jr (1965) Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase. J. Biol. Chem. 240: 4158-4163
    • (1965) J. Biol. Chem. , vol.240 , pp. 4158-4163
    • Webster Jr., L.T.1
  • 36
    • 0013815509 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction. 3. Evidence of a double requirement for divalent cations
    • Webster L. T. Jr (1965) Studies of the acetyl coenzyme A synthetase reaction. 3. Evidence of a double requirement for divalent cations. J. Biol. Chem. 240: 4164-4169
    • (1965) J. Biol. Chem. , vol.240 , pp. 4164-4169
    • Webster Jr., L.T.1
  • 37
    • 0014011751 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction. IV. The requirement for monovalent cations
    • Webster L. T. Jr (1966) Studies of the acetyl coenzyme A synthetase reaction. IV. The requirement for monovalent cations. J. Biol. Chem. 241: 5504-5510
    • (1966) J. Biol. Chem. , vol.241 , pp. 5504-5510
    • Webster Jr., L.T.1
  • 38
    • 0015618419 scopus 로고
    • The molecular weight and thiol residues of acetyl-coenzyme A synthetase from ox heart mitochondria
    • Londensborough J. C., Yuan S. L. and Webster L. T. Jr (1973) The molecular weight and thiol residues of acetyl-coenzyme A synthetase from ox heart mitochondria. Biochem. J. 133: 23-36
    • (1973) Biochem. J. , vol.133 , pp. 23-36
    • Londensborough, J.C.1    Yuan, S.L.2    Webster Jr., L.T.3
  • 39
    • 0016240928 scopus 로고
    • Equilibrium constants of the reactions of acetyl coenzyme A synthetase and the hydrolysis of adenosine triphosphate to adenosine monophosphate and inorganic pyrophosphate
    • Guynn R. W., Webster L. T. Jr and Veech R. L. (1974) Equilibrium constants of the reactions of acetyl coenzyme A synthetase and the hydrolysis of adenosine triphosphate to adenosine monophosphate and inorganic pyrophosphate. J. Biol. Chem. 249: 3248-3254
    • (1974) J. Biol. Chem. , vol.249 , pp. 3248-3254
    • Guynn, R.W.1    Webster Jr., L.T.2    Veech, R.L.3
  • 40
    • 0017350841 scopus 로고
    • Purification and properties of acetyl coenzyme A synthetase from bakers' yeast
    • Frenkel E. P. and Kitchens R. L. (1977) Purification and properties of acetyl coenzyme A synthetase from bakers' yeast. J. Biol. Chem. 252: 504-507
    • (1977) J. Biol. Chem. , vol.252 , pp. 504-507
    • Frenkel, E.P.1    Kitchens, R.L.2
  • 41
    • 0017287188 scopus 로고
    • Synthesis and properties of diastereoisomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate)
    • Eckstein F. and Goody R. S. (1976) Synthesis and properties of diastereoisomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate). Biochemistry 15: 1685-1691
    • (1976) Biochemistry , vol.15 , pp. 1685-1691
    • Eckstein, F.1    Goody, R.S.2
  • 42
    • 17344372249 scopus 로고    scopus 로고
    • Modified oligonucleotides: Synthesis and strategy for users
    • Verma S. and Eckstein F. (1998) Modified oligonucleotides: synthesis and strategy for users. Ann. Rev. Biochem. 67: 99-134
    • (1998) Ann. Rev. Biochem. , vol.67 , pp. 99-134
    • Verma, S.1    Eckstein, F.2
  • 43
    • 0018164638 scopus 로고
    • The stereochemical course of acetate activation by yeast acetyl-CoA synthetase
    • Midelfort C. F. and Sarton-Miller I. (1978) The stereochemical course of acetate activation by yeast acetyl-CoA synthetase. J. Biol. Chem. 253: 7127-7129
    • (1978) J. Biol. Chem. , vol.253 , pp. 7127-7129
    • Midelfort, C.F.1    Sarton-Miller, I.2
  • 44
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
    • Gulick A. M., Starai V. J., Horswill A. R., Homick K. M. and Escalante-Semerena J. C. (2003) The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry 42: 2866-2873
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 45
    • 1042276711 scopus 로고    scopus 로고
    • Crystal structure of yeast acetylcoenzyme A synthetase in complex with AMP
    • Jogl G. and Tong L. (2004) Crystal structure of yeast acetylcoenzyme A synthetase in complex with AMP. Biochemistry 43: 1425-1431
    • (2004) Biochemistry , vol.43 , pp. 1425-1431
    • Jogl, G.1    Tong, L.2
  • 46
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May J. J., Kessler N., Marahiel M. A. and Stubbs M. T. (2002) Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. USA 99: 12120-121205
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12120-121205
    • May, J.J.1    Kessler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 47
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S
    • Conti E., Stachelhaus T., Marahiel M. A. and Brick P. (1997) Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S. EMBO J. 16: 4174-4183
    • (1997) EMBO J. , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 48
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firely luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti E., Franks N. P. and Brick P. (1996) Crystal structure of firely luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4: 287-298
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 49
    • 0034625092 scopus 로고    scopus 로고
    • The role of lysine 529, a conserved residue of the acyl-adenylate- forming enzyme superfamily, in firefly luciferase
    • Branchini B. R., Murtiashaw M. H., Magyar R. A. and Anderson S. M. (2000) The role of lysine 529, a conserved residue of the acyl-adenylate- forming enzyme superfamily, in firefly luciferase. Biochemistry 39: 5433-5440
    • (2000) Biochemistry , vol.39 , pp. 5433-5440
    • Branchini, B.R.1    Murtiashaw, M.H.2    Magyar, R.A.3    Anderson, S.M.4
  • 50
    • 0037133231 scopus 로고    scopus 로고
    • Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: Residue Lys592 is required for propionyl-AMP synthesis
    • Horswill A. R. and Escalante-Semerena J. C. (2002) Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis. Biochemistry 41: 2379-2387
    • (2002) Biochemistry , vol.41 , pp. 2379-2387
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 51
    • 0035668493 scopus 로고    scopus 로고
    • Identification of active site residues in Bradyrhizobium japonicum acetyl-CoA synthetase
    • Tokyo
    • Lee H. Y., Na K. B., Koo H. M. and Kim Y. S. (2001) Identification of active site residues in Bradyrhizobium japonicum acetyl-CoA synthetase. J. Biochem. (Tokyo) 130: 807-813
    • (2001) J. Biochem. , vol.130 , pp. 807-813
    • Lee, H.Y.1    Na, K.B.2    Koo, H.M.3    Kim, Y.S.4
  • 53
    • 10744225021 scopus 로고    scopus 로고
    • The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli
    • Gimenez R., Nunez M. F., Badia J., Aguilar J. and Baldoma L. (2003) The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli. J. Bacteriol. 185: 6448-6455
    • (2003) J. Bacteriol. , vol.185 , pp. 6448-6455
    • Gimenez, R.1    Nunez, M.F.2    Badia, J.3    Aguilar, J.4    Baldoma, L.5
  • 54
    • 0033621553 scopus 로고    scopus 로고
    • Sigma(70) is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli
    • Kumari S., Simel E. J. and Wolfe A. J. (2000) Sigma(70) is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli. J. Bacteriol. 182: 551-554
    • (2000) J. Bacteriol. , vol.182 , pp. 551-554
    • Kumari, S.1    Simel, E.J.2    Wolfe, A.J.3
  • 55
    • 0042890424 scopus 로고    scopus 로고
    • Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism
    • Beatty C. M., Browning D. F., Busby S. J. and Wolfe A. J. (2003) Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism. J. Bacteriol. 185: 5148-5157
    • (2003) J. Bacteriol. , vol.185 , pp. 5148-5157
    • Beatty, C.M.1    Browning, D.F.2    Busby, S.J.3    Wolfe, A.J.4
  • 56
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby S. and Ebright R. H. (1999) Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 293: 199-213
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 57
    • 0346964255 scopus 로고    scopus 로고
    • Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: Anti-activation by the nucleoid proteins FIS and IHF
    • Browning D. F., Beatty C. M., Sanstad E. A., Gunn K. E., Busby S. J. and Wolfe A. J. (2004) Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: anti-activation by the nucleoid proteins FIS and IHF. Mol. Microbiol. 51: 241-254
    • (2004) Mol. Microbiol. , vol.51 , pp. 241-254
    • Browning, D.F.1    Beatty, C.M.2    Sanstad, E.A.3    Gunn, K.E.4    Busby, S.J.5    Wolfe, A.J.6
  • 58
    • 0026620949 scopus 로고
    • Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli
    • Ball C. A., Osuna R., Ferguson K. C. and Johnson R. C. (1992) Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli. J. Bacteriol. 174: 8043-8056
    • (1992) J. Bacteriol. , vol.174 , pp. 8043-8056
    • Ball, C.A.1    Osuna, R.2    Ferguson, K.C.3    Johnson, R.C.4
  • 59
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam T. A. and Ishihama A. (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274: 33105-33113
    • (1999) J. Biol. Chem. , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 60
    • 0037582107 scopus 로고    scopus 로고
    • Regulation of crp transcription by oscillation between distinct nucleoprotein complexes
    • Gonzalez-Gil G., Kahmann R. and Muskhelishvili G. (1998) Regulation of crp transcription by oscillation between distinct nucleoprotein complexes. EMBO J. 17: 2877-2885
    • (1998) EMBO J. , vol.17 , pp. 2877-2885
    • Gonzalez-Gil, G.1    Kahmann, R.2    Muskhelishvili, G.3
  • 61
    • 0035947613 scopus 로고    scopus 로고
    • CRP modulates fis transcription by alternate formation of activating and repressing nucleoprotein complexes
    • Nasser W., Schneider R., Travers A. and Muskhelishvili G. (2001) CRP modulates fis transcription by alternate formation of activating and repressing nucleoprotein complexes. J. Biol. Chem. 276: 17878-17886
    • (2001) J. Biol. Chem. , vol.276 , pp. 17878-17886
    • Nasser, W.1    Schneider, R.2    Travers, A.3    Muskhelishvili, G.4
  • 62
    • 0031034211 scopus 로고    scopus 로고
    • Involvement of iclR and rpoS in the induction of acs, the gene for acetyl coenzyme A synthetase of Escherichia coli K12
    • Shin S., Song S. G., Lee D. S., Pan J. G. and Park C. (1997) Involvement of iclR and rpoS in the induction of acs, the gene for acetyl coenzyme A synthetase of Escherichia coli K12. FEMS Microbiol. Lett. 146: 103-108
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 103-108
    • Shin, S.1    Song, S.G.2    Lee, D.S.3    Pan, J.G.4    Park, C.5
  • 63
    • 0032932220 scopus 로고    scopus 로고
    • Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis
    • Blankenhorn D., Phillips J. and Slonczewski J. L. (1999) Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis. J. Bacteriol. 181: 2209-2216
    • (1999) J. Bacteriol. , vol.181 , pp. 2209-2216
    • Blankenhorn, D.1    Phillips, J.2    Slonczewski, J.L.3
  • 64
    • 0348109341 scopus 로고    scopus 로고
    • CcpA-dependent carbon catabolite repression in bacteria
    • Warner J. B. and Lolkema J. S. (2003) CcpA-dependent carbon catabolite repression in bacteria. Microbiol. Mol. Biol. Rev. 67: 475-490
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 475-490
    • Warner, J.B.1    Lolkema, J.S.2
  • 65
    • 0030057004 scopus 로고    scopus 로고
    • The role of CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis
    • Henkin T. M. (1996) The role of CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis. FEMS Microbiol. Lett. 135: 9-15
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 9-15
    • Henkin, T.M.1
  • 66
    • 0018371990 scopus 로고
    • Effects of aeration on formation and localization of the acetyl coenzyme A synthetases of Saccharomyces cerevisiae
    • Klein H. P. and Jahnke L. (1979) Effects of aeration on formation and localization of the acetyl coenzyme A synthetases of Saccharomyces cerevisiae. J. Bacteriol. 137: 179-184
    • (1979) J. Bacteriol. , vol.137 , pp. 179-184
    • Klein, H.P.1    Jahnke, L.2
  • 67
    • 0030710569 scopus 로고    scopus 로고
    • Transcriptional control of the yeast acetyl-CoA synthetase gene, ACS1, by the positive regulators CAT8 and ADR1 and the pleiotropic repressor UME6
    • Kratzer S. and Schuller H. J. (1997) Transcriptional control of the yeast acetyl-CoA synthetase gene, ACS1, by the positive regulators CAT8 and ADR1 and the pleiotropic repressor UME6. Mol. Microbiol. 26: 631-641
    • (1997) Mol. Microbiol. , vol.26 , pp. 631-641
    • Kratzer, S.1    Schuller, H.J.2
  • 68
    • 0028302020 scopus 로고
    • A carbon source-responsive promoter element necessary for activation of the isocitrate lyase gene ICL1 is common to genes of the gluconeogenic pathway in the yeast Saccharomyces cerevisiae
    • Schöler A. and Schüller H. J. (1994) A carbon source-responsive promoter element necessary for activation of the isocitrate lyase gene ICL1 is common to genes of the gluconeogenic pathway in the yeast Saccharomyces cerevisiae. Mol. Cell Biol. 14: 3613-3622
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3613-3622
    • Schöler, A.1    Schüller, H.J.2
  • 69
    • 0030832065 scopus 로고    scopus 로고
    • Constitutive and carbon source-responsive promoter elements are involved in the regulated expression of the Saccharomyces cerevisiae malate synthase gene MLS1
    • Caspary F., Hartig A. and Schuller H. J. (1997) Constitutive and carbon source-responsive promoter elements are involved in the regulated expression of the Saccharomyces cerevisiae malate synthase gene MLS1. Mol. Gen. Genet. 255: 619-627
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 619-627
    • Caspary, F.1    Hartig, A.2    Schuller, H.J.3
  • 70
    • 0025965525 scopus 로고
    • Two monomers of yeast transcription factor ADR1 bind a palindromic sequence symmetrically to activate ADH2 expression
    • Thukral S. K., Eisen A. and Young E. T. (1991) Two monomers of yeast transcription factor ADR1 bind a palindromic sequence symmetrically to activate ADH2 expression. Mol. Cell Biol. 11: 1566-1577
    • (1991) Mol. Cell Biol. , vol.11 , pp. 1566-1577
    • Thukral, S.K.1    Eisen, A.2    Young, E.T.3
  • 71
    • 0028930777 scopus 로고
    • CAT8, a new zinc cluster-encoding gene necessary for derepression of gluconeogenic enzymes in the yeast Saccharomyces cerevisiae
    • Hedges D., Proft M. and Entian K. D. (1995) CAT8, a new zinc cluster-encoding gene necessary for derepression of gluconeogenic enzymes in the yeast Saccharomyces cerevisiae. Mol. Cell Biol. 15: 1915-1922
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1915-1922
    • Hedges, D.1    Proft, M.2    Entian, K.D.3
  • 72
    • 0030987084 scopus 로고    scopus 로고
    • Glucose derepression of gluconeogenic enzymes in Saccharomyces cerevisiae correlates with phosphorylation of the gene activator Cat8p
    • Randez-Gil F., Bojunga N., Proft M. and Entian K. D. (1997) Glucose derepression of gluconeogenic enzymes in Saccharomyces cerevisiae correlates with phosphorylation of the gene activator Cat8p. Mol. Cell Biol. 17: 2502-2510
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2502-2510
    • Randez-Gil, F.1    Bojunga, N.2    Proft, M.3    Entian, K.D.4
  • 73
    • 0034875093 scopus 로고    scopus 로고
    • Adr1 and Cat8 synergistically activate the glucose-regulated alcohol dehydrogenase gene ADH2 of the yeast Saccharomyces cerevisiae
    • Walther K. and Schuller H. J. (2001) Adr1 and Cat8 synergistically activate the glucose-regulated alcohol dehydrogenase gene ADH2 of the yeast Saccharomyces cerevisiae. Microbiology 147: 2037-2044
    • (2001) Microbiology , vol.147 , pp. 2037-2044
    • Walther, K.1    Schuller, H.J.2
  • 75
    • 0027321247 scopus 로고
    • The INO1 promoter of Saccharomyces cerevisiae includes an upstream repressor sequence (URS1) common to a diverse set of yeast genes
    • Lopes J. M., Schulze K. L., Yates J. W., Hirsch J. P. and Henry S. A. (1993) The INO1 promoter of Saccharomyces cerevisiae includes an upstream repressor sequence (URS1) common to a diverse set of yeast genes. J. Bacteriol. 175: 4235-4238
    • (1993) J. Bacteriol. , vol.175 , pp. 4235-4238
    • Lopes, J.M.1    Schulze, K.L.2    Yates, J.W.3    Hirsch, J.P.4    Henry, S.A.5
  • 76
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg M. L. and Lopes J. M. (1996) Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 60: 1-20
    • (1996) Microbiol. Rev. , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 77
    • 0027981960 scopus 로고
    • Importance of general regulatory factors Rap1p, Abf1p and Reb1p for the activation of yeast fatty acid synthase genes FAS1 and FAS2
    • Schüller H. J., Schutz A., Knab S., Hoffmann B. and Schweizer E. (1994) Importance of general regulatory factors Rap1p, Abf1p and Reb1p for the activation of yeast fatty acid synthase genes FAS1 and FAS2. Eur. J. Biochem. 225: 213-222
    • (1994) Eur. J. Biochem. , vol.225 , pp. 213-222
    • Schüller, H.J.1    Schutz, A.2    Knab, S.3    Hoffmann, B.4    Schweizer, E.5
  • 78
    • 0028216507 scopus 로고
    • Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: Identification of a functional UASINO and sequences responsible for fatty acid mediated repression
    • Chirala S. S., Zhong Q., Huang W. and al-Feel W. (1994) Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: identification of a functional UASINO and sequences responsible for fatty acid mediated repression. Nucleic Acids Res. 22: 412-418
    • (1994) Nucleic Acids Res. , vol.22 , pp. 412-418
    • Chirala, S.S.1    Zhong, Q.2    Huang, W.3    Al-Feel, W.4
  • 80
    • 0025011104 scopus 로고
    • ARS binding factor 1 binds adjacent to RAP1 at the UASs of the yeast glycolytic genes PGK and PYK1
    • Chambers A., Stanway C., Tsang J. S., Henry Y., Kingsman A. J. and Kingsman S. M. (1990) ARS binding factor 1 binds adjacent to RAP1 at the UASs of the yeast glycolytic genes PGK and PYK1. Nucleic Acids Res. 18: 5393-5399
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5393-5399
    • Chambers, A.1    Stanway, C.2    Tsang, J.S.3    Henry, Y.4    Kingsman, A.J.5    Kingsman, S.M.6
  • 81
    • 0034871773 scopus 로고    scopus 로고
    • Three target genes for the transcriptional activator Cat8p of Kluyveromyces lactis: Acetyl coenzyme A synthetase genes KlACS1 and KlACS2 and lactate permease gene KlJEN1
    • Lodi T., Saliola M., Donnini C. and Goffrini P. (2001) Three target genes for the transcriptional activator Cat8p of Kluyveromyces lactis: acetyl coenzyme A synthetase genes KlACS1 and KlACS2 and lactate permease gene KlJEN1. J. Bacteriol. 183: 5257-5261
    • (2001) J. Bacteriol. , vol.183 , pp. 5257-5261
    • Lodi, T.1    Saliola, M.2    Donnini, C.3    Goffrini, P.4
  • 82
    • 0032055886 scopus 로고    scopus 로고
    • FacB, the Aspergillus nidulans activator of acetate utilization genes, binds dissimilar DNA sequences
    • Todd R. B., Andrianopoulos A., Davis M. A. and Hynes M. J. (1998) FacB, the Aspergillus nidulans activator of acetate utilization genes, binds dissimilar DNA sequences. EMBO J. 17: 2042-2054
    • (1998) EMBO J. , vol.17 , pp. 2042-2054
    • Todd, R.B.1    Andrianopoulos, A.2    Davis, M.A.3    Hynes, M.J.4
  • 83
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein R., Carey M., Ptashne M. and Harrison S. C. (1992) DNA recognition by GAL4: structure of a protein-DNA complex. Nature 356: 408-414
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 84
    • 0034978613 scopus 로고    scopus 로고
    • Histone acetylation: Plants and fungi as model systems for the investigation of histone deacetylases
    • Graessle S., Loidl P. and Brosch G. (2001) Histone acetylation: plants and fungi as model systems for the investigation of histone deacetylases. Cell. Mol. Life Sci. 58: 704-720
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 704-720
    • Graessle, S.1    Loidl, P.2    Brosch, G.3
  • 85
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • Moazed D. (2001) Enzymatic activities of Sir2 and chromatin silencing. Curr. Opin. Cell Biol. 13: 232-238
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 232-238
    • Moazed, D.1
  • 86
    • 0024591141 scopus 로고
    • Evidence that the production of acetate in rat hepatocytes is a predominantly cytoplasmic process
    • Crabtree B., Souter M. J. and Anderson S. E. (1989) Evidence that the production of acetate in rat hepatocytes is a predominantly cytoplasmic process. Biochem. J. 257: 673-678
    • (1989) Biochem. J. , vol.257 , pp. 673-678
    • Crabtree, B.1    Souter, M.J.2    Anderson, S.E.3
  • 87
    • 0026022054 scopus 로고
    • The contribution of the large intestine to blood acetate in man
    • Scheppach W., Pomare E. W., Elia M. and Cummings J. H. (1991) The contribution of the large intestine to blood acetate in man. Clin. Sci. 80: 177-182
    • (1991) Clin. Sci. , vol.80 , pp. 177-182
    • Scheppach, W.1    Pomare, E.W.2    Elia, M.3    Cummings, J.H.4
  • 88
    • 0017363420 scopus 로고
    • Regulation of cytoplasmic acetyl-CoA and acetoacetyl-CoA synthetases by dexamethasone phosphate in rat liver and adipose tissue
    • Wolczunowicz M. and Rous S. (1977) Regulation of cytoplasmic acetyl-CoA and acetoacetyl-CoA synthetases by dexamethasone phosphate in rat liver and adipose tissue. Life Sci. 20: 1347-1352
    • (1977) Life Sci. , vol.20 , pp. 1347-1352
    • Wolczunowicz, M.1    Rous, S.2
  • 89
    • 0015525537 scopus 로고
    • Dietary changes of cytoplasmic acetyl-CoA synthetase in different rat tissues
    • Barth C., Sladek M. and Decker K. (1972) Dietary changes of cytoplasmic acetyl-CoA synthetase in different rat tissues. Biochim. Biophys. Acta 260: 1-9
    • (1972) Biochim. Biophys. Acta , vol.260 , pp. 1-9
    • Barth, C.1    Sladek, M.2    Decker, K.3
  • 90
    • 0034714382 scopus 로고    scopus 로고
    • Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins
    • Luong A., Hannah V. C., Brown M. S. and Goldstein J. L. (2000) Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J. Biol. Chem. 275: 26458-26466
    • (2000) J. Biol. Chem. , vol.275 , pp. 26458-26466
    • Luong, A.1    Hannah, V.C.2    Brown, M.S.3    Goldstein, J.L.4
  • 91
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • Edwards P. A. and Ericsson J. (1999) Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway. Annu. Rev. Biochem. 68: 157-185
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 92
    • 0032892175 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins: Activators of cholesterol and fatty acid biosynthesis
    • Horton J. D. and Shimomura I. (1999) Sterol regulatory element-binding proteins: activators of cholesterol and fatty acid biosynthesis. Curr. Opin. Lipidol. 10: 143-150
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 143-150
    • Horton, J.D.1    Shimomura, I.2
  • 93
    • 0034047473 scopus 로고    scopus 로고
    • The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds
    • Ke J., Behal R. H., Back S. L., Nikolau B. J., Wurtele E. S. and Oliver D. J. (2000) The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds. Plant Physiol. 123: 497-508
    • (2000) Plant Physiol. , vol.123 , pp. 497-508
    • Ke, J.1    Behal, R.H.2    Back, S.L.3    Nikolau, B.J.4    Wurtele, E.S.5    Oliver, D.J.6
  • 94
    • 12944283150 scopus 로고    scopus 로고
    • A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family
    • Smith J. S., Brachmann C. B., Celic I., Kenna M. A., Muhammad S. and Starai V. J. et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc. Natl. Acad. Sci. USA 97: 6658-6663
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6658-6663
    • Smith, J.S.1    Brachmann, C.B.2    Celic, I.3    Kenna, M.A.4    Muhammad, S.5    Starai, V.J.6
  • 95
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai V. J., Celic I., Cole R. N., Boeke J. D. and Escalante-Semerena J. C. (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298: 2390-2392
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 96
    • 1842582617 scopus 로고    scopus 로고
    • Fungal ammonia fermentation-A novel metabolic mechanism that couples the dissimilatory and assimilatory pathways of both nitrate and ethanol-Role of acetyl
    • Takasaki K., Shoun H., Yamaguchi M., Takeo K., Nakamura A. and Hoshino T. et al. (2004) Fungal ammonia fermentation-A novel metabolic mechanism that couples the dissimilatory and assimilatory pathways of both nitrate and ethanol-Role of acetyl. J. Biol. Chem. 279: 12414-12420
    • (2004) J. Biol. Chem. , vol.279 , pp. 12414-12420
    • Takasaki, K.1    Shoun, H.2    Yamaguchi, M.3    Takeo, K.4    Nakamura, A.5    Hoshino, T.6
  • 97
    • 0037297590 scopus 로고    scopus 로고
    • Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae
    • Starai V. J., Takahashi H., Boeke J. D. and Escalante-Semerena J. C. (2003) Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Genetics 163: 545-555
    • (2003) Genetics , vol.163 , pp. 545-555
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 98
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6- dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang A. W. and Escalante-Semerena J. C. (1998) CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J. Biol. Chem. 273: 31788-31794
    • (1998) J. Biol. Chem. , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 99
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD(+)-dependent deacetylation reactions
    • Sauve A. A., Celic I., Avalos J., Deng H., Boeke J. D. and Schramm V. L. (2001) Chemistry of gene silencing: the mechanism of NAD(+)-dependent deacetylation reactions. Biochemistry 40: 15456-15463
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 100
    • 0037166269 scopus 로고    scopus 로고
    • Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases
    • Jackson M. D. and Denu J. M. (2002) Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases. J. Biol. Chem. 277: 18535-18544
    • (2002) J. Biol. Chem. , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 101
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve A. A. and Schramm V. L. (2003) Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry 42: 9249-9256
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 102
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman K. J., Anderson R. M., Cohen H. Y., Latorre-Esteves M. and Sinclair D. A. (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277: 45099-45107
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 103
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • Jackson M. D., Schmidt M. T., Oppenheimer N. J. and Denu J. M. (2003) Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278: 50985-50998
    • (2003) J. Biol. Chem. , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 104
    • 0037221445 scopus 로고    scopus 로고
    • Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases
    • Denu J. M. (2003) Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases. Trends Biochem. Sci. 28: 41-48
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 41-48
    • Denu, J.M.1
  • 105
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression and chromosome stability
    • Brachmann C. B., Sherman J. M., Devine S. E., Cameron E. E., Pillus L. and Boeke J. D. (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression and chromosome stability. Genes Dev. 9: 2888-2902
    • (1995) Genes Dev. , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 106
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin S. J., Kaeberlein M., Andalis A. A., Sturtz L. A., Defossez P. A., Culotta V. C. et al. (2002) Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418: 344-348
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1    Kaeberlein, M.2    Andalis, A.A.3    Sturtz, L.A.4    Defossez, P.A.5    Culotta, V.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.