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Volumn 54, Issue 24, 2015, Pages 3860-3870

Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BINS; CARBOXYLATION; CATALYSIS; CRYSTAL STRUCTURE; ESTERIFICATION; ESTERS; FATTY ACIDS; POLYPEPTIDES; PROTEINS; REACTION INTERMEDIATES;

EID: 84934949330     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00340     Document Type: Article
Times cited : (14)

References (43)
  • 2
    • 0016830820 scopus 로고
    • Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification
    • Tanabe, T., Wada, K., Okazaki, T., and Numa, S. (1975) Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification Eur. J. Biochem. 57, 15-24
    • (1975) Eur. J. Biochem. , vol.57 , pp. 15-24
    • Tanabe, T.1    Wada, K.2    Okazaki, T.3    Numa, S.4
  • 3
    • 0036018143 scopus 로고    scopus 로고
    • Multi-subunit acetyl-CoA carboxylases
    • Cronan, J. E., Jr. and Waldrop, G. L. (2002) Multi-subunit acetyl-CoA carboxylases Prog. Lipid Res. 41, 407-435
    • (2002) Prog. Lipid Res. , vol.41 , pp. 407-435
    • Cronan, J.E.1    Waldrop, G.L.2
  • 4
    • 0024315260 scopus 로고
    • The Mechanism of Biotin-Dependent Enzymes
    • Knowles, J. R. (1989) The Mechanism of Biotin-Dependent Enzymes Annu. Rev. Biochem. 58, 195-221
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 6
    • 0022876079 scopus 로고
    • ATPase Activity of Biotin Carboxylase Provides Evidence for Initial Activation of HCO3- by ATP in the Carboxylation of Biotin
    • Climent, I. and Rubio, V. (1986) ATPase Activity of Biotin Carboxylase Provides Evidence for Initial Activation of HCO3- by ATP in the Carboxylation of Biotin Arch. Biochem. Biophys. 251, 465-470
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 465-470
    • Climent, I.1    Rubio, V.2
  • 7
    • 84867687720 scopus 로고    scopus 로고
    • The Enzymes of Biotin Dependent CO2 Metabolism: What Structures Reveal about their Reaction Mechanisms
    • Waldrop, G. L., St. Maurice, M., and Holden, H. M. (2012) The Enzymes of Biotin Dependent CO2 Metabolism: What Structures Reveal about their Reaction Mechanisms Protein Sci. 21, 1597-1619
    • (2012) Protein Sci. , vol.21 , pp. 1597-1619
    • Waldrop, G.L.1    St. Maurice, M.2    Holden, H.M.3
  • 9
    • 0031467818 scopus 로고    scopus 로고
    • (1997) A Diverse Superfamily of Enzymes with ATP-Dependent Carboxylate-Amine/Thiol Ligase Activity
    • Galperin, M. Y. and Koonin, E. V. (1997) (1997) A Diverse Superfamily of Enzymes with ATP-Dependent Carboxylate-Amine/Thiol Ligase Activity Protein Sci. 6, 2639-2643
    • (1997) Protein Sci. , vol.6 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.2
  • 10
    • 0028085434 scopus 로고
    • Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA Carboxylase
    • Waldrop, G. L., Rayment, I., and Holden, H. M. (1994) Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA Carboxylase Biochemistry 33, 10249-10256
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 11
    • 0034717247 scopus 로고    scopus 로고
    • Movement of the Biotin Carboxylase B-Domain as a Result of ATP Binding
    • Thoden, J. B., Blanchard, C. Z., Holden, H. M., and Waldrop, G. L. (2000) Movement of the Biotin Carboxylase B-Domain as a Result of ATP Binding J. Biol. Chem. 275, 16183-16190
    • (2000) J. Biol. Chem. , vol.275 , pp. 16183-16190
    • Thoden, J.B.1    Blanchard, C.Z.2    Holden, H.M.3    Waldrop, G.L.4
  • 12
    • 52949102964 scopus 로고    scopus 로고
    • Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase
    • Mochalkin, I., Miller, J. R., Evdokimov, A., Lightle, S., Yan, C., Stover, C. K., and Waldrop, G. L. (2008) Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase Protein Sci. 17, 1706-1718
    • (2008) Protein Sci. , vol.17 , pp. 1706-1718
    • Mochalkin, I.1    Miller, J.R.2    Evdokimov, A.3    Lightle, S.4    Yan, C.5    Stover, C.K.6    Waldrop, G.L.7
  • 13
    • 66349100742 scopus 로고    scopus 로고
    • Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism
    • Chou, C. Y., Yu, L. P., and Tong, L. (2009) Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism J. Biol. Chem. 284, 11690-11697
    • (2009) J. Biol. Chem. , vol.284 , pp. 11690-11697
    • Chou, C.Y.1    Yu, L.P.2    Tong, L.3
  • 15
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans, P. R. (2006) Scaling and assessment of data quality Acta Crystallogr. D62, 72-82
    • (2006) Acta Crystallogr. , vol.62 , pp. 72-82
    • Evans, P.R.1
  • 17
    • 0028103275 scopus 로고
    • The Ccp4 suite: Programs for protein crystallography
    • Bailey, S. (1994) The Ccp4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
    • Bailey, S.1
  • 18
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 19
    • 0033574251 scopus 로고    scopus 로고
    • Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin
    • Blanchard, C. Z., Lee, Y. M., Frantom, P. A., and Waldrop, G. L. (1999) Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin Biochemistry 38, 3393-3400
    • (1999) Biochemistry , vol.38 , pp. 3393-3400
    • Blanchard, C.Z.1    Lee, Y.M.2    Frantom, P.A.3    Waldrop, G.L.4
  • 20
    • 0023885546 scopus 로고
    • Catalytic mechanism of biotin carboxylase: Steady-state kinetic investigations
    • Tipton, P. A. and Cleland, W. W. (1988) Catalytic mechanism of biotin carboxylase: Steady-state kinetic investigations Biochemistry 27, 4317-4325
    • (1988) Biochemistry , vol.27 , pp. 4317-4325
    • Tipton, P.A.1    Cleland, W.W.2
  • 21
    • 0023691809 scopus 로고
    • On the intermediacy of carboxyphosphate in biotin-dependent carboxylations
    • Ogita, T. and Knowles, J. R. (1988) On the intermediacy of carboxyphosphate in biotin-dependent carboxylations Biochemistry 27, 8028-8033
    • (1988) Biochemistry , vol.27 , pp. 8028-8033
    • Ogita, T.1    Knowles, J.R.2
  • 22
    • 0000806739 scopus 로고
    • Alcohol-Bicarbonate-Water System. Structure-Reactivity Studies on the Equilibriums for Formation of Alkyl Monocarbonates and on the Rates of Their Decomposition in Aqueous Alkali
    • Sauers, C. K., Jencks, W. P., and Groh, S. (1975) Alcohol-Bicarbonate-Water System. Structure-Reactivity Studies on the Equilibriums for Formation of Alkyl Monocarbonates and on the Rates of Their Decomposition in Aqueous Alkali J. Am. Chem. Soc. 97, 5546-5553
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 5546-5553
    • Sauers, C.K.1    Jencks, W.P.2    Groh, S.3
  • 23
    • 0015522507 scopus 로고
    • On the Possible Involvement of a Carbonyl Phosphate Intermediate in the Adenosine Triphosphate-dependent Carboxylation of Biotin
    • Polakis, S. E., Guchhait, R. B., and Lane, M. D. (1972) On the Possible Involvement of a Carbonyl Phosphate Intermediate in the Adenosine Triphosphate-dependent Carboxylation of Biotin J. Biol. Chem. 247, 1335-1337
    • (1972) J. Biol. Chem. , vol.247 , pp. 1335-1337
    • Polakis, S.E.1    Guchhait, R.B.2    Lane, M.D.3
  • 24
    • 80755174401 scopus 로고    scopus 로고
    • Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli
    • Lietzan, A. D., Menefee, A. L., Zeczycki, T. N., Kumar, S., Attwood, P. V., Wallace, J. C., Cleland, W. W., and St Maurice, M. (2011) Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli Biochemistry 50, 9708-9723
    • (2011) Biochemistry , vol.50 , pp. 9708-9723
    • Lietzan, A.D.1    Menefee, A.L.2    Zeczycki, T.N.3    Kumar, S.4    Attwood, P.V.5    Wallace, J.C.6    Cleland, W.W.7    St Maurice, M.8
  • 25
    • 0000631410 scopus 로고
    • Mechanisms of Decarboxylation of Carboxybiotin
    • Tipton, P. A. and Cleland, W. W. (1988) Mechanisms of Decarboxylation of Carboxybiotin J. Am. Chem. Soc. 110, 5866-5869
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5866-5869
    • Tipton, P.A.1    Cleland, W.W.2
  • 26
    • 73049129684 scopus 로고
    • Zur Biochemischen Funktion des Biotin
    • Knappe, J., Ringermann, E., and Lynen, F. (1961) Zur Biochemischen Funktion des Biotin Biochem. Z. 335, 168-176
    • (1961) Biochem. Z. , vol.335 , pp. 168-176
    • Knappe, J.1    Ringermann, E.2    Lynen, F.3
  • 27
    • 0018990373 scopus 로고
    • Molecular Structure and Intermolecular Interactions of N1′-Methoxycarbonylbiotin Methyl Ester: A Model for Carboxybiotin
    • Stallings, W. C., Monti, C. T., Lane, M. D., and DeTitta, G. T. (1980) Molecular Structure and Intermolecular Interactions of N1′-Methoxycarbonylbiotin Methyl Ester: A Model for Carboxybiotin Proc. Natl. Acad. Sci. U.S.A. 77, 1260-1264
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1260-1264
    • Stallings, W.C.1    Monti, C.T.2    Lane, M.D.3    Detitta, G.T.4
  • 29
    • 0024286069 scopus 로고
    • Carbon-13 and Deuterium Isotope Effects on the Catalytic Reactions of Biotin Carboxylase
    • Tipton, P. A. and Cleland, W. W. (1988) Carbon-13 and Deuterium Isotope Effects on the Catalytic Reactions of Biotin Carboxylase Biochemistry 27, 4325-4332
    • (1988) Biochemistry , vol.27 , pp. 4325-4332
    • Tipton, P.A.1    Cleland, W.W.2
  • 30
    • 0034636083 scopus 로고    scopus 로고
    • Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?
    • Levert, K. L., Lloyd, R. B., and Waldrop, G. L. (2000) Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin? Biochemistry 39, 4122-4128
    • (2000) Biochemistry , vol.39 , pp. 4122-4128
    • Levert, K.L.1    Lloyd, R.B.2    Waldrop, G.L.3
  • 31
    • 84865437643 scopus 로고    scopus 로고
    • Inverse Solvent Isotope Effects Demonstrate Slow Aquo Release from Hypoxia Inducible Factor-Prolyl Hydroxylase (PDH2)
    • Flagg, S. C., Giri, N., Pektas, S., Maroney, M. J., and Knapp, M. J. (2012) Inverse Solvent Isotope Effects Demonstrate Slow Aquo Release from Hypoxia Inducible Factor-Prolyl Hydroxylase (PDH2) Biochemistry 51, 6654-6666
    • (2012) Biochemistry , vol.51 , pp. 6654-6666
    • Flagg, S.C.1    Giri, N.2    Pektas, S.3    Maroney, M.J.4    Knapp, M.J.5
  • 32
    • 0026455197 scopus 로고
    • Mechanistic studies on the human matrix metalloproteinase stromelysin
    • Harrison, R. K., Chang, B., Niedzwiecki, L., and Stein, R. L. (1992) Mechanistic studies on the human matrix metalloproteinase stromelysin Biochemistry 31, 10757-10762
    • (1992) Biochemistry , vol.31 , pp. 10757-10762
    • Harrison, R.K.1    Chang, B.2    Niedzwiecki, L.3    Stein, R.L.4
  • 33
    • 0032555189 scopus 로고    scopus 로고
    • Hydrolysis of N-succinyl- l, l -diaminopimelic acid by the Haemophilus influenza dapE-encoded desuccinylase: Metal activation, solvent isotope effects, and kinetic mechanism
    • Born, T. L., Zheng, R. J., and Blanchard, J. S. (1998) Hydrolysis of N-succinyl- l, l -diaminopimelic acid by the Haemophilus influenza dapE-encoded desuccinylase: Metal activation, solvent isotope effects, and kinetic mechanism Biochemistry 37, 10478-10487
    • (1998) Biochemistry , vol.37 , pp. 10478-10487
    • Born, T.L.1    Zheng, R.J.2    Blanchard, J.S.3
  • 34
    • 1942501809 scopus 로고    scopus 로고
    • Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase
    • Sloane, V. and Waldrop, G. L. (2004) Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase J. Biol. Chem. 279, 15772-15778
    • (2004) J. Biol. Chem. , vol.279 , pp. 15772-15778
    • Sloane, V.1    Waldrop, G.L.2
  • 35
    • 0001177474 scopus 로고
    • Enzymic Carboxyl Transfer from N-Carboxybioitn. A Molecular Orbital Evaluation of Conformational Effects in Promoting Reactivity
    • Thatcher, G. R. J., Poirier, R., and Kluger, R. (1986) Enzymic Carboxyl Transfer from N-Carboxybioitn. A Molecular Orbital Evaluation of Conformational Effects in Promoting Reactivity J. Am. Chem. Soc. 108, 2699-2704
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2699-2704
    • Thatcher, G.R.J.1    Poirier, R.2    Kluger, R.3
  • 36
    • 0023272362 scopus 로고
    • Proton Exchange in Biotin: A Reinvestigation, with Implications for the Mechanism of CO2 Transfer
    • Perrin, C. L. and Dwyer, T. J. (1987) Proton Exchange in Biotin: A Reinvestigation, with Implications for the Mechanism of CO2 Transfer J. Am. Chem. Soc. 109, 5163-5167
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5163-5167
    • Perrin, C.L.1    Dwyer, T.J.2
  • 37
    • 37049106453 scopus 로고
    • Intramolecular Nucleophilic Attack on Carboxylate by Ureide Anion. General Acid-Base Catalysis of the Alkaline Cyclisation of 2,2,3,5-Tetramethylhydantoic Acid
    • Blagoeva, I. B., Pojarlieff, I. G., and Kirby, A. J. (1984) Intramolecular Nucleophilic Attack on Carboxylate by Ureide Anion. General Acid-Base Catalysis of the Alkaline Cyclisation of 2,2,3,5-Tetramethylhydantoic Acid J. Chem. Soc., Perkin Trans. 2, 745-751
    • (1984) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 745-751
    • Blagoeva, I.B.1    Pojarlieff, I.G.2    Kirby, A.J.3
  • 38
    • 0028151598 scopus 로고
    • Vancomycin Resistance: Structure of d -Alanine: D -Alanine Ligase at 2.3 Å Resolution
    • Fan, C., Moews, P. C., Walsh, C. T., and Knox, J. R. (1994) Vancomycin Resistance: Structure of d -Alanine: d -Alanine Ligase at 2.3 Å Resolution Science 266, 439-443
    • (1994) Science , vol.266 , pp. 439-443
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 39
    • 0032406042 scopus 로고    scopus 로고
    • Carbamoyl Phosphate Synthetase from Escherichia coli Does Not Catalyze the Dehydration of Bicarbonate to Carbon Dioxide
    • Gibson, G. E., Mullins, L. S., and Raushel, F. M. (1998) Carbamoyl Phosphate Synthetase from Escherichia coli Does Not Catalyze the Dehydration of Bicarbonate to Carbon Dioxide Bioorg. Chem. 26, 255-268
    • (1998) Bioorg. Chem. , vol.26 , pp. 255-268
    • Gibson, G.E.1    Mullins, L.S.2    Raushel, F.M.3


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