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Volumn 32, Issue 2, 2007, Pages 1195-1206

Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate

Author keywords

Crystal structure; L threonine; Propionate metabolism; Structure function relationship

Indexed keywords

ENZYME; PHOSPHATE ACETYLTRANSFERASE; PROPIONIC ACID; THREONINE; THREONINE DEHYDRATASE;

EID: 35348859006     PISSN: 02505991     EISSN: 02505991     Source Type: Journal    
DOI: 10.1007/s12038-007-0121-1     Document Type: Review
Times cited : (22)

References (66)
  • 1
    • 0014963054 scopus 로고
    • A phosphoenzyme intermediary in acetate kinase action
    • Anthony R S and Spector L B 1970 A phosphoenzyme intermediary in acetate kinase action; J. Biol. Chem. 245 6739-6741
    • (1970) J. Biol. Chem , vol.245 , pp. 6739-6741
    • Anthony, R.S.1    Spector, L.B.2
  • 3
    • 0037131403 scopus 로고    scopus 로고
    • X-ray structure of pyruvate formatelyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage
    • Becker A and Kabsch W 2002 X-ray structure of pyruvate formatelyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage; J. Biol. Chem. 277 40036-40042
    • (2002) J. Biol. Chem , vol.277 , pp. 40036-40042
    • Becker, A.1    Kabsch, W.2
  • 4
    • 0017879034 scopus 로고
    • Allosteric inhibition and catabolite inactivation of purified biodegradative threonine dehydratase of Salmonella typhimurium
    • Bhadra R and Datta P 1978 Allosteric inhibition and catabolite inactivation of purified biodegradative threonine dehydratase of Salmonella typhimurium; Biochemistry 17 1691-1699
    • (1978) Biochemistry , vol.17 , pp. 1691-1699
    • Bhadra, R.1    Datta, P.2
  • 5
    • 0018781487 scopus 로고
    • 18O] triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase
    • 18O] triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase; Biochemistry 18 3927-3933
    • (1979) Biochemistry , vol.18 , pp. 3927-3933
    • Blattler, W.A.1    Knowles, J.R.2
  • 6
    • 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
    • 0014348405 scopus 로고
    • Role of pyruvate and Sadenosylmethionine in activating the pyruvate formate-lyase of Escherichia coli
    • Chase T, Jr. and Rabinowitz J C 1968 Role of pyruvate and Sadenosylmethionine in activating the pyruvate formate-lyase of Escherichia coli; J. Bacteriol. 96 1065-1078
    • (1968) J. Bacteriol , vol.96 , pp. 1065-1078
    • Chase Jr., T.1    Rabinowitz, J.C.2
  • 8
    • 0030835705 scopus 로고    scopus 로고
    • Involvement of FNR and ArcA in anaerobic expression of the tdc operon of Escherichia coli
    • Chattopadhyay S, Wu Y, and Datta P 1997 Involvement of FNR and ArcA in anaerobic expression of the tdc operon of Escherichia coli; J. Bacteriol. 179 4868-4873
    • (1997) J. Bacteriol , vol.179 , pp. 4868-4873
    • Chattopadhyay, S.1    Wu, Y.2    Datta, P.3
  • 10
    • 0016414179 scopus 로고
    • L-threonine dehydrase as a model of allosteric control involving ligand-induced oligomerization
    • Dunne C P and Wood W A 1975 L-threonine dehydrase as a model of allosteric control involving ligand-induced oligomerization; Curr. Top. Cell Regul. 9 65-101
    • (1975) Curr. Top. Cell Regul , vol.9 , pp. 65-101
    • Dunne, C.P.1    Wood, W.A.2
  • 11
    • 0026095288 scopus 로고
    • Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli
    • Eisenstein E 1991 Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli; J. Biol. Chem. 266 5801-5807
    • (1991) J. Biol. Chem , vol.266 , pp. 5801-5807
    • Eisenstein, E.1
  • 12
    • 0016813478 scopus 로고
    • Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli
    • Feldman D A and Datta P 1975 Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli; Biochemistry 14 1760-1767
    • (1975) Biochemistry , vol.14 , pp. 1760-1767
    • Feldman, D.A.1    Datta, P.2
  • 13
    • 0028275314 scopus 로고
    • 2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site
    • 2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site; J. Biol. Chem. 269 12432-12437
    • (1994) J. Biol. Chem , vol.269 , pp. 12432-12437
    • Frey, M.1    Rothe, M.2    Wagner, A.F.3    Knappe, J.4
  • 14
    • 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 Grishin N V 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
  • 15
    • 0027443625 scopus 로고
    • TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins
    • Ganduri Y L, Sadda S R, Datta M W, Jambukeswaran R K and Datta P 1993 TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins; Mol. Gen. Genet. 240 395-402
    • (1993) Mol. Gen. Genet , vol.240 , pp. 395-402
    • Ganduri, Y.L.1    Sadda, S.R.2    Datta, M.W.3    Jambukeswaran, R.K.4    Datta, P.5
  • 16
    • 0015766283 scopus 로고
    • The mechanism of action of 5′-adenylic acid-activated threonine dehydrase. V. Relation between ligand-induced allosteric activation and the protomer-oligomer interconversion
    • Gerlt J A, Rabinowitz K W, Dunne C P and Wood W A 1973 The mechanism of action of 5′-adenylic acid-activated threonine dehydrase. V. Relation between ligand-induced allosteric activation and the protomer-oligomer interconversion; J. Biol. Chem. 248 8200-8206
    • (1973) J. Biol. Chem , vol.248 , pp. 8200-8206
    • Gerlt, J.A.1    Rabinowitz, K.W.2    Dunne, C.P.3    Wood, W.A.4
  • 17
    • 15444365167 scopus 로고    scopus 로고
    • Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila
    • Gorrell A, Lawrence S H and Ferry J G 2005 Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila; J. Biol. Chem. 280 10731-10742
    • (2005) J. Biol. Chem , vol.280 , pp. 10731-10742
    • Gorrell, A.1    Lawrence, S.H.2    Ferry, J.G.3
  • 18
    • 0031973793 scopus 로고    scopus 로고
    • Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
    • Hesslinger C, Fairhurst S A and Sawers G 1998 Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate; Mol. Microbiol. 27 477-492
    • (1998) Mol. Microbiol , vol.27 , pp. 477-492
    • Hesslinger, C.1    Fairhurst, S.A.2    Sawers, G.3
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, Thompson J D, Higgins D G and Gibson T J 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
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 20
    • 15244359850 scopus 로고    scopus 로고
    • Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase
    • Ingram-Smith C, Gorrell A, Lawrence S H, Iyer P, Smith K and Ferry J G 2005 Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase; J. Bacteriol. 187 2386-2394
    • (2005) J. Bacteriol , vol.187 , pp. 2386-2394
    • Ingram-Smith, C.1    Gorrell, A.2    Lawrence, S.H.3    Iyer, P.4    Smith, K.5    Ferry, J.G.6
  • 22
    • 0016294957 scopus 로고
    • Pyruvate formate-lyase of Escherichia coli: The acetyl-enzyme intermediate
    • Knappe J, Blaschkowski H P, Grobner P and Schmitt T 1974 Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate; Eur. J. Biochem. 50 253-263
    • (1974) Eur. J. Biochem , vol.50 , pp. 253-263
    • Knappe, J.1    Blaschkowski, H.P.2    Grobner, P.3    Schmitt, T.4
  • 24
    • 31344456182 scopus 로고    scopus 로고
    • Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila
    • Lawrence S H and Ferry J G 2006 Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila; J. Bacteriol. 188 1155-1158
    • (2006) J. Bacteriol , vol.188 , pp. 1155-1158
    • Lawrence, S.H.1    Ferry, J.G.2
  • 25
    • 31344437517 scopus 로고    scopus 로고
    • Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila
    • Lawrence S H, Luther K B, Schindelin H and Ferry J G 2006 Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila; J. Bacteriol. 188 1143-1154
    • (2006) J. Bacteriol , vol.188 , pp. 1143-1154
    • Lawrence, S.H.1    Luther, K.B.2    Schindelin, H.3    Ferry, J.G.4
  • 27
    • 0016197875 scopus 로고
    • Biodegradative L-threonine deaminase of Salmonella typhimurium
    • Luginbuhl G H, Hofler J G, Decedue C J and Burns R O 1974 Biodegradative L-threonine deaminase of Salmonella typhimurium; J. Bacteriol. 120 559-561
    • (1974) J. Bacteriol , vol.120 , pp. 559-561
    • Luginbuhl, G.H.1    Hofler, J.G.2    Decedue, C.J.3    Burns, R.O.4
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0037151123 scopus 로고    scopus 로고
    • Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila
    • Miles R D, Gorrell A and Ferry J G 2002 Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila; J. Biol. Chem. 277 22547-22552
    • (2002) J. Biol. Chem , vol.277 , pp. 22547-22552
    • Miles, R.D.1    Gorrell, A.2    Ferry, J.G.3
  • 31
    • 0035976897 scopus 로고    scopus 로고
    • Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila
    • Miles R D, Iyer P P and Ferry J G 2001 Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila; J. Biol. Chem. 276 45059-45064
    • (2001) J. Biol. Chem , vol.276 , pp. 45059-45064
    • Miles, R.D.1    Iyer, P.P.2    Ferry, J.G.3
  • 32
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J and Changeux J P 1965 On the nature of allosteric transitions: a plausible model; J. Mol. Biol. 12 88-118
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 33
    • 0014198966 scopus 로고
    • Studies on the interaction between regulatory enzymes and effectors. I. Effect of adenosine 5′-monophosphate analogues on threonine deaminase
    • Nakazawa A, Tokushige M, Hayaishi O, Ikehara M and Mizuno Y 1967 Studies on the interaction between regulatory enzymes and effectors. I. Effect of adenosine 5′-monophosphate analogues on threonine deaminase; J. Biol. Chem. 242 3868-3872
    • (1967) J. Biol. Chem , vol.242 , pp. 3868-3872
    • Nakazawa, A.1    Tokushige, M.2    Hayaishi, O.3    Ikehara, M.4    Mizuno, Y.5
  • 34
    • 0018424838 scopus 로고
    • Inhibition of Escherichia coli biodegradative threonine dehydratase by pyruvate
    • Park L S and Datta P 1979 Inhibition of Escherichia coli biodegradative threonine dehydratase by pyruvate; J. Bacteriol. 138 1026-1028
    • (1979) J. Bacteriol , vol.138 , pp. 1026-1028
    • Park, L.S.1    Datta, P.2
  • 35
    • 0015369402 scopus 로고
    • Kinetic properties of phosphotransacetylase from Veillonella alcalescens
    • Pelroy R A and Whiteley H R 1972 Kinetic properties of phosphotransacetylase from Veillonella alcalescens; J. Bacteriol. 111 47-55.
    • (1972) J. Bacteriol , vol.111 , pp. 47-55
    • Pelroy, R.A.1    Whiteley, H.R.2
  • 36
    • 0014429761 scopus 로고
    • The mechanism of action of 5′-adenylic acid-activated threonine dehydratase. III. Structural requirements for nucleotide allosteric activation
    • Rabinowitz K W, Shada J D and Wood W A 1968 The mechanism of action of 5′-adenylic acid-activated threonine dehydratase. III. Structural requirements for nucleotide allosteric activation; J. Biol. Chem. 243 3214-3217
    • (1968) J. Biol. Chem , vol.243 , pp. 3214-3217
    • Rabinowitz, K.W.1    Shada, J.D.2    Wood, W.A.3
  • 37
    • 0015856129 scopus 로고
    • Phosphotransacetylase from Bacillus subtilis: Purification and physiological studies
    • Rado T A and Hoch J A 1973 Phosphotransacetylase from Bacillus subtilis: purification and physiological studies; Biochim. Biophys. Acta 321 114-125
    • (1973) Biochim. Biophys. Acta , vol.321 , pp. 114-125
    • Rado, T.A.1    Hoch, J.A.2
  • 38
    • 0032454701 scopus 로고    scopus 로고
    • The anaerobic degradation of L-serine and L-threonine in enterobacteria: Networks of pathways and regulatory signals
    • Sawers G 1998 The anaerobic degradation of L-serine and L-threonine in enterobacteria: networks of pathways and regulatory signals; Arch. Microbiol. 171 1-5
    • (1998) Arch. Microbiol , vol.171 , pp. 1-5
    • Sawers, G.1
  • 39
    • 0035103230 scopus 로고    scopus 로고
    • A novel mechanism controls anaerobic and catabolite regulation of the Escherichia coli tdc operon
    • Sawers G 2001 A novel mechanism controls anaerobic and catabolite regulation of the Escherichia coli tdc operon; Mol. Microbiol. 39 1285-1298
    • (2001) Mol. Microbiol , vol.39 , pp. 1285-1298
    • Sawers, G.1
  • 40
    • 0032448106 scopus 로고    scopus 로고
    • The glycyl radical enzyme TdcE can replace pyruvate formate-lyase in glucose fermentation
    • Sawers G, Hesslinger C, Muller N and Kaiser M 1998 The glycyl radical enzyme TdcE can replace pyruvate formate-lyase in glucose fermentation; J. Bacteriol. 180 3509-3516
    • (1998) J. Bacteriol , vol.180 , pp. 3509-3516
    • Sawers, G.1    Hesslinger, C.2    Muller, N.3    Kaiser, M.4
  • 41
    • 0024441334 scopus 로고
    • Identification and DNA sequence of tdcR, a positive regulatory gene of the tdc operon of Escherichia coli
    • Schweizer H P and Datta P 1989 Identification and DNA sequence of tdcR, a positive regulatory gene of the tdc operon of Escherichia coli; Mol. Gen. Genet. 218 516-522
    • (1989) Mol. Gen. Genet , vol.218 , pp. 516-522
    • Schweizer, H.P.1    Datta, P.2
  • 42
    • 0014622054 scopus 로고
    • Phosphotransacetylase of Escherichia coli B, purification and properties
    • Shimizu M, Suzuki T, Kameda K Y and Abiko Y 1969 Phosphotransacetylase of Escherichia coli B, purification and properties; Biochim. Biophys. Acta 191 550-558
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 550-558
    • Shimizu, M.1    Suzuki, T.2    Kameda, K.Y.3    Abiko, Y.4
  • 43
    • 0017222290 scopus 로고
    • Regulation of biodegradative threonine deaminase
    • Shizuta Y and Hayaishi O 1976 Regulation of biodegradative threonine deaminase; Curr. Top. Cell Regul. 11 99-146
    • (1976) Curr. Top. Cell Regul , vol.11 , pp. 99-146
    • Shizuta, Y.1    Hayaishi, O.2
  • 44
    • 0015935175 scopus 로고
    • Regulation of biodegradative threonine deaminase. I. Allosteric inhibition of the enzyme by a reaction product and its reversal by adenosine 5′-monophosphate
    • Shizuta Y, Kurosawa A, Inoue K, Tanabe T and Hayaishi O 1973 Regulation of biodegradative threonine deaminase. I. Allosteric inhibition of the enzyme by a reaction product and its reversal by adenosine 5′-monophosphate; J. Biol. Chem. 248 512-520
    • (1973) J. Biol. Chem , vol.248 , pp. 512-520
    • Shizuta, Y.1    Kurosawa, A.2    Inoue, K.3    Tanabe, T.4    Hayaishi, O.5
  • 45
    • 24644481814 scopus 로고    scopus 로고
    • Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: Comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily
    • Simanshu D K, Savithri H S and Murthy M R 2005 Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily; J. Mol. Biol. 352 876-892
    • (2005) J. Mol. Biol , vol.352 , pp. 876-892
    • Simanshu, D.K.1    Savithri, H.S.2    Murthy, M.R.3
  • 46
    • 33845991866 scopus 로고    scopus 로고
    • Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation
    • Simanshu D K, Savithri H S and Murthy M R 2006 Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation; J. Biol. Chem. 281 39630-39641
    • (2006) J. Biol. Chem , vol.281 , pp. 39630-39641
    • Simanshu, D.K.1    Savithri, H.S.2    Murthy, M.R.3
  • 48
    • 0011063236 scopus 로고
    • Acetate kinase: A triple-displacement enzyme
    • Spector L B 1980 Acetate kinase: a triple-displacement enzyme; Proc. Natl. Acad. Sci. USA 77 2626-2630
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2626-2630
    • Spector, L.B.1
  • 49
    • 0014633973 scopus 로고
    • Phosphotransacetylase of Escherichia coli B, activation by pyruvate and inhibition by NADH and certain nucleotides
    • Suzuki T 1969 Phosphotransacetylase of Escherichia coli B, activation by pyruvate and inhibition by NADH and certain nucleotides; Biochim. Biophys. Acta 191 559-569
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 559-569
    • Suzuki, T.1
  • 50
    • 0014669760 scopus 로고
    • Activation and inhibition of purified phosphotransacetylase of Escherichia coli B by pyruvate and by NADH2 and certain nucleotides
    • Suzuki T, Abiko Y and Shimizu M 1969 Activation and inhibition of purified phosphotransacetylase of Escherichia coli B by pyruvate and by NADH2 and certain nucleotides; Biochem. Biophys. Res. Commun. 35 102-108
    • (1969) Biochem. Biophys. Res. Commun , vol.35 , pp. 102-108
    • Suzuki, T.1    Abiko, Y.2    Shimizu, M.3
  • 52
    • 0345273884 scopus 로고
    • Threonine deamination in Escherichia coli II. Evidence for two L-threonine deaminases
    • Umbarger E and Brown B 1957 Threonine deamination in Escherichia coli II. Evidence for two L-threonine deaminases; J. Bacteriol. 73 105-112
    • (1957) J. Bacteriol , vol.73 , pp. 105-112
    • Umbarger, E.1    Brown, B.2
  • 53
    • 0001348712 scopus 로고    scopus 로고
    • Biosynthesis of branched-chain amino acids
    • eds F C Neidhardt, R Curtiss III, J L Ingraham, E C C Lin, K B Low, B Magasanik, W S Reznikoff, M Riley, M Schaechter, H E Umbarger et al (Washington DC: American Society for Microbiology Press) pp
    • Umbarger H E 1996 Biosynthesis of branched-chain amino acids; in Escherichia coli and Salmonella typhimurium: cellular and molecular biology (eds) F C Neidhardt, R Curtiss III, J L Ingraham, E C C Lin, K B Low, B Magasanik, W S Reznikoff, M Riley, M Schaechter, H E Umbarger et al (Washington DC: American Society for Microbiology Press) pp 442-457
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and molecular biology , pp. 442-457
    • Umbarger, H.E.1
  • 54
    • 0024460702 scopus 로고
    • The free radical of pyruvate formate-lyase. Characterization by EPR spectroscopy and involvement in catalysis as studied with the substrate-analogue hypophosphite
    • Unkrig V, Neugebauer F A and Knappe J 1989 The free radical of pyruvate formate-lyase. Characterization by EPR spectroscopy and involvement in catalysis as studied with the substrate-analogue hypophosphite; Eur. J. Biochem. 184 723-728
    • (1989) Eur. J. Biochem , vol.184 , pp. 723-728
    • Unkrig, V.1    Neugebauer, F.A.2    Knappe, J.3
  • 55
    • 0023278164 scopus 로고
    • Involvement of ack-pta operon products in alpha-ketobutyrate metabolism by Salmonella typhimurium
    • Van Dyk T K and LaRossa R A 1987 Involvement of ack-pta operon products in alpha-ketobutyrate metabolism by Salmonella typhimurium; Mol. Gen. Genet. 207 435-440
    • (1987) Mol. Gen. Genet , vol.207 , pp. 435-440
    • Van Dyk, T.K.1    LaRossa, R.A.2
  • 56
    • 0020959230 scopus 로고
    • 4-tetraphosphate: A pleiotropically acting alarmone?
    • 4-tetraphosphate: a pleiotropically acting alarmone? Cell 34 711-712
    • (1983) Cell , vol.34 , pp. 711-712
    • Varshavsky, A.1
  • 58
    • 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
  • 59
    • 0014408205 scopus 로고
    • The mechanism of action of 5′-adenylic acid-activated threonine dehydrase. II. Protomer-oligomer interconversions and related properties
    • Whanger P D, Phillips A T, Rabinowitz K W, Piperno J R, Shada J D and Wood W A 1968 The mechanism of action of 5′-adenylic acid-activated threonine dehydrase. II. Protomer-oligomer interconversions and related properties; J. Biol. Chem. 243 167-173
    • (1968) J. Biol. Chem , vol.243 , pp. 167-173
    • Whanger, P.D.1    Phillips, A.T.2    Rabinowitz, K.W.3    Piperno, J.R.4    Shada, J.D.5    Wood, W.A.6
  • 60
    • 0010750369 scopus 로고
    • Serine and threonine deaminases of Escherichia coli: Activators for a cell-free enzyme
    • Wood W A and Gunsalus I C 1949 Serine and threonine deaminases of Escherichia coli: activators for a cell-free enzyme; J. Biol. Chem. 181 171-182
    • (1949) J. Biol. Chem , vol.181 , pp. 171-182
    • Wood, W.A.1    Gunsalus, I.C.2
  • 61
    • 0026608772 scopus 로고
    • Integration host factor is required for positive regulation of the tdc operon of Escherichia coli
    • Wu Y F and Datta P 1992 Integration host factor is required for positive regulation of the tdc operon of Escherichia coli; J. Bacteriol. 174 233-240
    • (1992) J. Bacteriol , vol.174 , pp. 233-240
    • Wu, Y.F.1    Datta, P.2
  • 62
    • 0026731955 scopus 로고
    • Catabolite gene activator protein and integration host factor act in concert to regulate tdc operon expression in Escherichia coli
    • Wu Y F, Patil R V and Datta P 1992 Catabolite gene activator protein and integration host factor act in concert to regulate tdc operon expression in Escherichia coli; J. Bacteriol. 174 6918-6927
    • (1992) J. Bacteriol , vol.174 , pp. 6918-6927
    • Wu, Y.F.1    Patil, R.V.2    Datta, P.3
  • 63
    • 1842531891 scopus 로고    scopus 로고
    • Crystal structure of a phosphotransacetylase from Streptococcus pyogenes
    • Xu Q S, Shin D H, Pufan R, Yokota H, Kim R and Kim S H 2004 Crystal structure of a phosphotransacetylase from Streptococcus pyogenes; Proteins 55 479-481
    • (2004) Proteins , vol.55 , pp. 479-481
    • Xu, Q.S.1    Shin, D.H.2    Pufan, R.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 66
    • 0028933966 scopus 로고
    • Active site residues of human brain hexokinase as studied by site-specific mutagenesis
    • Zeng C and Fromm H J 1995 Active site residues of human brain hexokinase as studied by site-specific mutagenesis; J. Biol. Chem. 270 10509-10513
    • (1995) J. Biol. Chem , vol.270 , pp. 10509-10513
    • Zeng, C.1    Fromm, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.