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Volumn 47, Issue 24, 2008, Pages 6322-6328

Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; AMINO ACIDS; BIOCHEMISTRY; CATALYSIS; HYDROGEN; METAL ANALYSIS; MICROFLUIDICS;

EID: 45749125616     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800075c     Document Type: Article
Times cited : (9)

References (16)
  • 1
    • 0014011576 scopus 로고
    • The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium
    • Kredich, N. M., and Tomkins, G. M. (1966) The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241, 4955-4965.
    • (1966) J. Biol. Chem , vol.241 , pp. 4955-4965
    • Kredich, N.M.1    Tomkins, G.M.2
  • 2
    • 0015217099 scopus 로고
    • Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)
    • Smith, I. K., and Thompson, J. F. (1971) Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris). Biochim. Biophys. Acta 227, 288-295.
    • (1971) Biochim. Biophys. Acta , vol.227 , pp. 288-295
    • Smith, I.K.1    Thompson, J.F.2
  • 3
    • 0027121143 scopus 로고
    • Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme
    • Vaara, M. (1992) Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme. FEMS Microbiol. Lett. 76, 249-254.
    • (1992) FEMS Microbiol. Lett , vol.76 , pp. 249-254
    • Vaara, M.1
  • 4
    • 0027181134 scopus 로고
    • The PROSITE dictionary of sites and patterns in proteins, its current status
    • Bairoch, A. (1993) The PROSITE dictionary of sites and patterns in proteins, its current status. Nucleic Acids Res. 21, 3097-3103.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3097-3103
    • Bairoch, A.1
  • 5
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R., and Roderick, S. L. (1995) A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.1    Roderick, S.L.2
  • 6
    • 4143109064 scopus 로고    scopus 로고
    • Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae
    • Johnson, C. M., Huang, B., Roderick, S. L., and Cook, P. F. (2004) Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Arch. Biochem. Biophys. 429, 115-122.
    • (2004) Arch. Biochem. Biophys , vol.429 , pp. 115-122
    • Johnson, C.M.1    Huang, B.2    Roderick, S.L.3    Cook, P.F.4
  • 7
    • 10644245071 scopus 로고    scopus 로고
    • Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae
    • Johnson, C. M., Huang, B., Roderick, S. L., and Cook, P. F. (2004) Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae. Biochemistry 43, 15534-15539.
    • (2004) Biochemistry , vol.43 , pp. 15534-15539
    • Johnson, C.M.1    Huang, B.2    Roderick, S.L.3    Cook, P.F.4
  • 8
    • 2442644099 scopus 로고    scopus 로고
    • Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor
    • Olsen, L. R., Huang, B., Vetting, M. W., and Roderick, S. L. (2004) Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor. Biochemistry 43, 6013-6019.
    • (2004) Biochemistry , vol.43 , pp. 6013-6019
    • Olsen, L.R.1    Huang, B.2    Vetting, M.W.3    Roderick, S.L.4
  • 9
    • 9744250218 scopus 로고    scopus 로고
    • The serine acetyltransferase reaction: Acetyl transfer from an acylpantothenyl donor to an alcohol
    • Johnson, C. M., Roderick, S. L., and Cook, P. F. (2005) The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Arch. Biochem. Biophys. 433, 85-95.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 85-95
    • Johnson, C.M.1    Roderick, S.L.2    Cook, P.F.3
  • 10
    • 16644396746 scopus 로고    scopus 로고
    • Structure of serine acetyltransferase from Haemophilus influenzae Rd
    • Gorman, J., and Shapiro, L. (2004) Structure of serine acetyltransferase from Haemophilus influenzae Rd. Acta Crystallogr. D 60, 1600-1605.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1600-1605
    • Gorman, J.1    Shapiro, L.2
  • 11
    • 0018265576 scopus 로고
    • Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers
    • Cook, P. F., and Wedding, R. T. (1978) Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. J. Biol. Chem. 253, 7874-7879.
    • (1978) J. Biol. Chem , vol.253 , pp. 7874-7879
    • Cook, P.F.1    Wedding, R.T.2
  • 13
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt, D. W. (1963) An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Indust. Appl. Math. 11, 431-441.
    • (1963) J. Soc. Indust. Appl. Math , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 14
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 15
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv. Enzymol. Relat. Areas Mol. Biol. 45, 273-387.
    • (1977) Adv. Enzymol. Relat. Areas Mol. Biol , vol.45 , pp. 273-387
    • Cleland, W.W.1
  • 16
    • 0033593224 scopus 로고    scopus 로고
    • Reaction mechanism of fructose-2, 6-bisphosphatase. A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway
    • Mizuguchi, H., Cook, P. F., Tai, C.-H., Hasemann, C. A., and Uyeda, K. (1999) Reaction mechanism of fructose-2, 6-bisphosphatase. A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway. J. Biol. Chem. 274, 2166-2175.
    • (1999) J. Biol. Chem , vol.274 , pp. 2166-2175
    • Mizuguchi, H.1    Cook, P.F.2    Tai, C.-H.3    Hasemann, C.A.4    Uyeda, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.