메뉴 건너뛰기




Volumn 451, Issue 2, 2013, Pages 205-216

Aminolaevulinic acid synthase of rhodobacter capsulatus: High-resolution kinetic investigation of the structural basis for substrate binding and catalysis

Author keywords

5 aminolaevulinic acid synthase (ALAS); Haem biosynthesis; Quinonoid intermediate formation; Steady state kinetics; Stopped flow spectroscopy

Indexed keywords

ALANINE; AMINO ACID; AMINOLAEVULINIC ACID SYNTHASE; AMINOLEVULINIC ACID; BACTERIAL ENZYME; GENOMIC DNA; QUINONE DERIVATIVE; STRUCTURAL PROTEIN; SUCCINYL COENZYME A; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84875628518     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121041     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • Eliot, A. C. and Kirsch, J. F. (2004) Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu. Rev. Biochem. 73, 383-415
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 2
    • 80054705398 scopus 로고    scopus 로고
    • Controlling reaction specificity in pyridoxal phosphate enzymes
    • Toney, M. D. (2011) Controlling reaction specificity in pyridoxal phosphate enzymes. Biochim. Biophys. Acta 1814, 1407-1418
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1407-1418
    • Toney, M.D.1
  • 3
    • 25144499698 scopus 로고    scopus 로고
    • Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to xlsa in humans
    • Astner, I., Schulze, J. O., van den Heuvel, J., Jahn, D., Schubert, W. D. and Heinz, D. W. (2005) Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. EMBO J. 24, 3166-3177
    • (2005) EMBO J. , vol.24 , pp. 3166-3177
    • Astner, I.1    Schulze, J.O.2    Van Den Heuvel, J.3    Jahn, D.4    Schubert, W.D.5    Heinz, D.W.6
  • 5
    • 77952721977 scopus 로고    scopus 로고
    • Structure and function of enzymes in heme biosynthesis
    • Layer, G., Reichelt, J., Jahn, D. and Heinz, D. W. (2010) Structure and function of enzymes in heme biosynthesis. Protein Sci. 19, 1137-1161
    • (2010) Protein Sci. , Issue.19 , pp. 1137-1161
    • Layer, G.1    Reichelt, J.2    Jahn, D.3    Heinz, D.W.4
  • 6
    • 0030054651 scopus 로고    scopus 로고
    • Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation
    • Tan, D. and Ferreira, G. C. (1996) Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation. Biochemistry 35, 8934-8941
    • (1996) Biochemistry , vol.35 , pp. 8934-8941
    • Tan, D.1    Ferreira, G.C.2
  • 7
    • 70349335786 scopus 로고    scopus 로고
    • Hereditary sideroblastic anemias: Pathophysiology, diagnosis, and treatment
    • Camaschella, C. (2009) Hereditary sideroblastic anemias: pathophysiology, diagnosis, and treatment. Semin. Hematol. 46, 371-377
    • (2009) Semin. Hematol. , vol.46 , pp. 371-377
    • Camaschella, C.1
  • 8
    • 69249096519 scopus 로고    scopus 로고
    • Arg85 and thr430 in murine 5-aminolevulinate synthase coordinate acyl-coa-binding and contribute to substrate specificity
    • Lendrihas, T., Zhang, J., Hunter, G. A. and Ferreira, G. C. (2009) Arg85 and Thr430 in murine 5-aminolevulinate synthase coordinate acyl-CoA-binding and contribute to substrate specificity. Protein Sci. 18, 1847-1859
    • (2009) Protein Sci. , vol.18 , pp. 1847-1859
    • Lendrihas, T.1    Zhang, J.2    Hunter, G.A.3    Ferreira, G.C.4
  • 9
    • 0027371956 scopus 로고
    • Heme biosynthesis in mammalian systems: Evidence of a schiff base linkage between the pyridoxal 5-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase
    • Ferreira, G. C., Neame, P. J. and Dailey, H. A. (1993) Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase. Protein Sci. 2, 1959-1965
    • (1993) Protein Sci. , vol.2 , pp. 1959-1965
    • Ferreira, G.C.1    Neame, P.J.2    Dailey, H.A.3
  • 10
    • 0028917375 scopus 로고
    • A continuous spectrophotometric assay for 5-aminolevulinate synthase that utilizes substrate cycling
    • Hunter, G. A. and Ferreira, G. C. (1995) A continuous spectrophotometric assay for 5-aminolevulinate synthase that utilizes substrate cycling. Anal. Biochem. 226, 221-224
    • (1995) Anal. Biochem. , vol.226 , pp. 221-224
    • Hunter, G.A.1    Ferreira, G.C.2
  • 11
    • 80054689577 scopus 로고    scopus 로고
    • Pyridoxal-5-phosphate-dependent enzymes involved in biotin biosynthesis: Structure, reaction mechanism and inhibition
    • Mann, S. and Ploux, O. (2011) Pyridoxal-5-phosphate-dependent enzymes involved in biotin biosynthesis: structure, reaction mechanism and inhibition. Biochim. Biophys. Acta 1814, 1459-1466
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1459-1466
    • Mann, S.1    Ploux, O.2
  • 12
    • 80054716155 scopus 로고    scopus 로고
    • Mechanistic enzymology of serine palmitoyltransferase
    • Ikushiro, H. and Hayashi, H. (2011) Mechanistic enzymology of serine palmitoyltransferase. Biochim. Biophys. Acta 1814, 1474-1480
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1474-1480
    • Ikushiro, H.1    Hayashi, H.2
  • 13
    • 84861518863 scopus 로고    scopus 로고
    • Structural, mechanistic and regulatory studies of serine palmitoyltransferase
    • Lowther, J., Naismith, J. H., Dunn, T. M. and Campopiano, D. J. (2012) Structural, mechanistic and regulatory studies of serine palmitoyltransferase. Biochem. Soc. Trans. 40, 547-554
    • (2012) Biochem. Soc. Trans. , Issue.40 , pp. 547-554
    • Lowther, J.1    Naismith, J.H.2    Dunn, T.M.3    Campopiano, D.J.4
  • 14
    • 0023665217 scopus 로고
    • Purification, properties, and n-terminal amino acid sequence of homogeneous escherichia coli 2-amino-3-ketobutyrate coa ligase, a pyridoxal phosphate-dependent enzyme
    • Mukherjee, J. J. and Dekker, E. E. (1987) Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme. J. Biol. Chem. 262, 14441-14447
    • (1987) J. Biol. Chem. , vol.262 , pp. 14441-14447
    • Mukherjee, J.J.1    Dekker, E.E.2
  • 15
    • 0035340280 scopus 로고    scopus 로고
    • Three-dimensional structure of 2-amino-3-ketobutyrate coa ligase from escherichia coli complexed with a plp-substrate intermediate: Inferred reaction mechanism
    • Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J. A., Smith, C., Matte, A., Schrag, J. D. and Cygler, M. (2001) Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry 40, 5151-5160
    • (2001) Biochemistry , vol.40 , pp. 5151-5160
    • Schmidt, A.1    Sivaraman, J.2    Li, Y.3    Larocque, R.4    Barbosa, J.A.5    Smith, C.6    Matte, A.7    Schrag, J.D.8    Cygler, M.9
  • 16
  • 17
    • 0037680229 scopus 로고    scopus 로고
    • Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism
    • Hanada, K. (2003) Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim. Biophys. Acta 1632, 16-30
    • (2003) Biochim. Biophys. Acta , vol.1632 , pp. 16-30
    • Hanada, K.1
  • 18
    • 0942290628 scopus 로고    scopus 로고
    • Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors
    • Ikushiro, H., Hayashi, H. and Kagamiyama, H. (2004) Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors. Biochemistry 43, 1082-1092
    • (2004) Biochemistry , vol.43 , pp. 1082-1092
    • Ikushiro, H.1    Hayashi, H.2    Kagamiyama, H.3
  • 19
    • 0032573591 scopus 로고    scopus 로고
    • The crystal structure of 8-amino-7-oxononanoate synthase: A bacterial plp-dependent, acyl-coa-condensing enzyme
    • Alexeev, D., Alexeeva, M., Baxter, R. L., Campopiano, D. J., Webster, S. P. and Sawyer, L. (1998) The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284, 401-419
    • (1998) J. Mol. Biol. , vol.284 , pp. 401-419
    • Alexeev, D.1    Alexeeva, M.2    Baxter, R.L.3    Campopiano, D.J.4    Webster, S.P.5    Sawyer, L.6
  • 20
    • 67449111212 scopus 로고    scopus 로고
    • 5-Aminolevulinate synthase: Catalysis of the first step of heme biosynthesis
    • Hunter, G. A. and Ferreira, G. C. (2009) 5-Aminolevulinate synthase: catalysis of the first step of heme biosynthesis. Cell. Mol. Biol. 55, 102-110
    • (2009) Cell. Mol. Biol. , Issue.55 , pp. 102-110
    • Hunter, G.A.1    Ferreira, G.C.2
  • 21
    • 33645454058 scopus 로고    scopus 로고
    • Mechanism of α-oxoamine synthases: Identification of the intermediate claisen product in the 8-amino-7-oxononanoate synthase reaction
    • Kerbarh, O., Campopiano, D. J. and Baxter, R. L. (2006) Mechanism of α-oxoamine synthases: identification of the intermediate Claisen product in the 8-amino-7-oxononanoate synthase reaction. Chem. Commun. 1, 60-62
    • (2006) Chem. Commun. , Issue.1 , pp. 60-62
    • Kerbarh, O.1    Campopiano, D.J.2    Baxter, R.L.3
  • 22
    • 0015721994 scopus 로고
    • 5-Aminolevulinic-acid synthetase of Rhodopseudomonas spheroides Y. Purification and some properties
    • Fanica-Gaignier, M. and Clement-Metral, J. (1973) 5-Aminolevulinic-acid synthetase of Rhodopseudomonas spheroides Y. Purification and some properties. Eur. J. Biochem. 40, 13-18
    • (1973) Eur. J. Biochem. , vol.40 , pp. 13-18
    • Fanica-Gaignier, M.1    Clement-Metral, J.2
  • 23
    • 0017855450 scopus 로고
    • δ-Aminolevulinic acid synthase of Rhodopseudomonas spheroides. Binding of pyridoxal phosphate to the enzyme
    • Nandi, D. L. (1978) δ-Aminolevulinic acid synthase of Rhodopseudomonas spheroides. Binding of pyridoxal phosphate to the enzyme. Arch. Biochem. Biophys. 188, 266-271
    • (1978) Arch. Biochem. Biophys. , vol.188 , pp. 266-271
    • Nandi, D.L.1
  • 25
    • 70349321700 scopus 로고    scopus 로고
    • D-amino acids govern stationary phase cell wall remodeling in bacteria
    • Lam, H., Oh, D. C., Cava, F., Takacs, C. N., Clardy, J., de Pedro, M. A. and Waldor, M. K. (2009) D-Amino acids govern stationary phase cell wall remodeling in bacteria. Science 325, 1552-1555
    • (2009) Science , vol.325 , pp. 1552-1555
    • Lam, H.1    Oh, D.2    Cava, F.3    Takacs, C.4    Clardy, J.5    De Pedro, M.6    Waldor, M.7
  • 27
    • 0037160011 scopus 로고    scopus 로고
    • Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism
    • Zhang, J. and Ferreira, G. C. (2002) Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism. J. Biol. Chem. 277, 44660-44669
    • (2002) J. Biol. Chem. , vol.277 , pp. 44660-44669
    • Zhang, J.1    Ferreira, G.C.2
  • 28
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of kinsim: A flexible, portable system
    • Barshop, B. A., Wrenn, R. F. and Frieden, C. (1983) Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM: a flexible, portable system. Anal. Biochem. 130, 134-145
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 29
    • 34548148701 scopus 로고    scopus 로고
    • Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase
    • Hunter, G. A., Zhang, J. and Ferreira, G. C. (2007) Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase. J. Biol. Chem. 282, 23025-23035
    • (2007) J. Biol. Chem. , Issue.282 , pp. 23025-23035
    • Hunter, G.A.1    Zhang, J.2    Ferreira, G.C.3
  • 30
    • 0033617165 scopus 로고    scopus 로고
    • Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release
    • Hunter, G. A. and Ferreira, G. C. (1999) Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release. J. Biol. Chem. 274, 12222-12228
    • (1999) J. Biol. Chem. , Issue.274 , pp. 12222-12228
    • Hunter, G.A.1    Ferreira, G.C.2
  • 31
    • 33748752708 scopus 로고    scopus 로고
    • Broad substrate stereospecificity of the mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies
    • Bhor, V. M., Dev, S., Vasanthakumar, G. R., Kumar, P., Sinha, S. and Surolia, A. (2006) Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: spectroscopic and kinetic studies. J. Biol. Chem. 281, 25076-25088
    • (2006) J. Biol. Chem. , Issue.281 , pp. 25076-25088
    • Bhor, V.M.1    Dev, S.2    Vasanthakumar, G.3    Kumar, P.4    Sinha, S.5    Surolia, A.6
  • 32
    • 43149103420 scopus 로고    scopus 로고
    • Acceleration of the substrate cα deprotonation by an analogue of the second substrate palmitoyl-coa in serine palmitoyltransferase
    • Ikushiro, H., Fujii, S., Shiraiwa, Y. and Hayashi, H. (2008) Acceleration of the substrate Cα deprotonation by an analogue of the second substrate palmitoyl-CoA in serine palmitoyltransferase. J. Biol. Chem. 283, 7542-7553
    • (2008) J. Biol. Chem. , vol.283 , pp. 7542-7553
    • Ikushiro, H.1    Fujii, S.2    Shiraiwa, Y.3    Hayashi, H.4
  • 33
    • 0022559020 scopus 로고
    • Purification of 5-aminolevulinate synthase
    • Jordan, P. M. and Laghai-Newton, A. (1986) Purification of 5-aminolevulinate synthase. Methods Enzymol. 123, 435-443
    • (1986) Methods Enzymol. , vol.123 , pp. 435-443
    • Jordan, P.M.1    Laghai-Newton, A.2
  • 34
    • 0032502324 scopus 로고    scopus 로고
    • Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5-phosphate cofactor
    • Gong, J., Hunter, G. A. and Ferreira, G. C. (1998) Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5-phosphate cofactor. Biochemistry 37, 3509-3517
    • (1998) Biochemistry , vol.37 , pp. 3509-3517
    • Gong, J.1    Hunter, G.A.2    Ferreira, G.C.3
  • 35
    • 0030855155 scopus 로고    scopus 로고
    • Continuous coupled assay for 5-aminolevulinate synthase
    • Shoolingin-Jordan, P. M., LeLean, J. E. and Lloyd, A. J. (1997) Continuous coupled assay for 5-aminolevulinate synthase. Methods Enzymol. 281, 309-316
    • (1997) Methods Enzymol. , vol.281 , pp. 309-316
    • Shoolingin-Jordan, P.M.1    LeLean, J.E.2    Lloyd, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.