메뉴 건너뛰기




Volumn 28, Issue 2, 1997, Pages 183-193

Role of electrostatics at the catalytic metal binding site in xylose isomerase action: Ca2+-inhibition and metal competence in the double mutant D254E/D256E

Author keywords

D xylose isomerase; Enzyme kinetics; Protein crystallography

Indexed keywords

BERYLLIUM; CALCIUM ION; GLUTAMIC ACID; MAGNESIUM ION; MANGANESE; METAL; XYLITOL; XYLOSE ISOMERASE;

EID: 0343683331     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<183::AID-PROT7>3.0.CO;2-G     Document Type: Article
Times cited : (20)

References (44)
  • 4
    • 0001304049 scopus 로고
    • X-ray analysis of D-xylose isomerase at 1.9 Å: Native enzyme in complex with substrate and with a mechanism-designed inactivator
    • Carrell, H.L., Glusker, J.P., Burger, V., Manfre, F., Tritsch, D., Biellmann, J.-F. X-ray analysis of D-xylose isomerase at 1.9 Å: Native enzyme in complex with substrate and with a mechanism-designed inactivator. Proc. Natl. Acad. Sci. U.S.A. 86:4440-4444, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4440-4444
    • Carrell, H.L.1    Glusker, J.P.2    Burger, V.3    Manfre, F.4    Tritsch, D.5    Biellmann, J.-F.6
  • 5
    • 0025974544 scopus 로고
    • A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose
    • Whitlow, M., Howard, A.J., Finzel, B.C., Poulos, T.L., Winborne, E., Gilliland, G.L. A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose. Proteins 9:153-173, 1991.
    • (1991) Proteins , vol.9 , pp. 153-173
    • Whitlow, M.1    Howard, A.J.2    Finzel, B.C.3    Poulos, T.L.4    Winborne, E.5    Gilliland, G.L.6
  • 6
    • 0024362334 scopus 로고
    • Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 Å and 2.3 Å resolution, respectively
    • Henrick, K., Collyer, C.A., Blow, D.M. Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 Å and 2.3 Å resolution, respectively. J. Mol. Biol. 208:129-157, 1989.
    • (1989) J. Mol. Biol. , vol.208 , pp. 129-157
    • Henrick, K.1    Collyer, C.A.2    Blow, D.M.3
  • 7
    • 0025320312 scopus 로고
    • Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift
    • Collyer, C.A., Henrick, K., Blow, D.M. Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift. J. Mol. Biol. 212:211-235, 1990.
    • (1990) J. Mol. Biol. , vol.212 , pp. 211-235
    • Collyer, C.A.1    Henrick, K.2    Blow, D.M.3
  • 9
    • 0028197040 scopus 로고
    • Isotopic exchange plus substrate and inhibition kinetics of D-xylose isomerase do not support a proton-transfer mechanism
    • Allen, K.N., Lavie, A., Farber, G.K., Glasfeld, A., Petsko, G.A., Ringe, D. Isotopic exchange plus substrate and inhibition kinetics of D-xylose isomerase do not support a proton-transfer mechanism. Biochemistry 33:1481-1487, 1994.
    • (1994) Biochemistry , vol.33 , pp. 1481-1487
    • Allen, K.N.1    Lavie, A.2    Farber, G.K.3    Glasfeld, A.4    Petsko, G.A.5    Ringe, D.6
  • 10
    • 0028953745 scopus 로고
    • Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex
    • Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D. Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex. Biochemistry 34:3742-3749, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3742-3749
    • Allen, K.N.1    Lavie, A.2    Petsko, G.A.3    Ringe, D.4
  • 11
    • 0026603050 scopus 로고
    • Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase
    • Rangarajan, M., Hartley, B.S. Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase. Biochem. J. 283:223-233, 1992.
    • (1992) Biochem. J. , vol.283 , pp. 223-233
    • Rangarajan, M.1    Hartley, B.S.2
  • 13
    • 0026723802 scopus 로고
    • Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis
    • van Tilbeurgh, H., Jenkins, J., Chiadmi, M., Janin, J., Wodak, S., Mrabet, N.T., Lambeir, A.M. Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis. Biochemistry 31:5467-5471, 1992.
    • (1992) Biochemistry , vol.31 , pp. 5467-5471
    • Van Tilbeurgh, H.1    Jenkins, J.2    Chiadmi, M.3    Janin, J.4    Wodak, S.5    Mrabet, N.T.6    Lambeir, A.M.7
  • 14
    • 0026750215 scopus 로고
    • Molecular mechanics simulations of a conformational rearrangement of D-xylose in the active site of D-xylose isomerase
    • Smart, O.S., Akins, J., Blow, D.M. Molecular mechanics simulations of a conformational rearrangement of D-xylose in the active site of D-xylose isomerase. Proteins 13:100-111, 1992.
    • (1992) Proteins , vol.13 , pp. 100-111
    • Smart, O.S.1    Akins, J.2    Blow, D.M.3
  • 15
    • 0027249189 scopus 로고
    • Theoretical examination of the mechanism of aldose-ketose isomerization
    • Zheng, Y.J., Merz, K.M., Jr., Farber, G.K. Theoretical examination of the mechanism of aldose-ketose isomerization. Prot. Engn. 6:479-486, 1993.
    • (1993) Prot. Engn. , vol.6 , pp. 479-486
    • Zheng, Y.J.1    Merz Jr., K.M.2    Farber, G.K.3
  • 16
    • 4243855963 scopus 로고
    • The role of electrostatics in the ring opening step of xylose isomerase catalysis
    • Fábián, P., Asbóth, B., Náray-Szabó, G. The role of electrostatics in the ring opening step of xylose isomerase catalysis. J. Mol. Struct. THEOCHEM 307:171-178, 1994.
    • (1994) J. Mol. Struct. THEOCHEM , vol.307 , pp. 171-178
    • Fábián, P.1    Asbóth, B.2    Náray-Szabó, G.3
  • 17
    • 0025116430 scopus 로고
    • Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes: Characterization of a structural gene and function of active site histidine
    • Lee, C., Bagdasarian, M., Meng, M., Zeikus, J.G. Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes: Characterization of a structural gene and function of active site histidine. J. Biol. Chem. 265: 19082-19090, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19082-19090
    • Lee, C.1    Bagdasarian, M.2    Meng, M.3    Zeikus, J.G.4
  • 18
    • 0029561175 scopus 로고
    • Molecular modelling of xylose isomerase catalysis: The role of electrostatics and charge transfer to metals
    • Fuxreiter, M., Farkas, Ö., Náray-Szabó, G. Molecular modelling of xylose isomerase catalysis: The role of electrostatics and charge transfer to metals. Prot. Eng. 8:925-933, 1995.
    • (1995) Prot. Eng. , vol.8 , pp. 925-933
    • Fuxreiter, M.1    Farkas, Ö.2    Náray-Szabó, G.3
  • 20
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U.S.A. 82:488-492, 1985.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 21
    • 0342368477 scopus 로고
    • Doctoral thesis. Cambridge University, England
    • Gibson, T.J. Doctoral thesis. Cambridge University, England, 1984.
    • (1984)
    • Gibson, T.J.1
  • 23
    • 0021073779 scopus 로고
    • Construction of improved M13 vectors using oligonucleotide-directed mutagenesis
    • Norrander, J., Kempe, T., Messing, J. Construction of improved M13 vectors using oligonucleotide-directed mutagenesis. Gene 26:101-106, 1983.
    • (1983) Gene , vol.26 , pp. 101-106
    • Norrander, J.1    Kempe, T.2    Messing, J.3
  • 25
    • 0025912071 scopus 로고
    • D-xylose (D-glucose) isomerase from Arthrobacter strain NRRL B3728. Purification and properties
    • Smith, C.A., Rangarajan, M., Hartley, B.S. D-xylose (D-glucose) isomerase from Arthrobacter strain NRRL B3728. Purification and properties. Biochem. J. 277:255-261, 1991.
    • (1991) Biochem. J. , vol.277 , pp. 255-261
    • Smith, C.A.1    Rangarajan, M.2    Hartley, B.S.3
  • 26
    • 0026760851 scopus 로고    scopus 로고
    • Stability of Arthrobacter D-xylose isomerase to denaturants and heat
    • Rangarajan, M., Asbóth, B., Hartley, B.S. Stability of Arthrobacter D-xylose isomerase to denaturants and heat. Biochem. J. 285:889-898.
    • Biochem. J. , vol.285 , pp. 889-898
    • Rangarajan, M.1    Asbóth, B.2    Hartley, B.S.3
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacament
    • Navaza, J. AMoRe: An automated package for molecular replacament. Acta Crystallogr. A50:157-163, 1994.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D50:760-763, 1994.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 31
    • 0002860357 scopus 로고
    • Diamond, R., Ramesseshan, S., Venkatesan, K. (eds.). Bangalore: Indian Academy of Sciences
    • Hendrickson, W.A., Konnert, J.H. In: "Computing in Crystallography." Diamond, R., Ramesseshan, S., Venkatesan, K. (eds.). Bangalore: Indian Academy of Sciences, 1980: 1301-1323.
    • (1980) Computing in Crystallography , pp. 1301-1323
    • Hendrickson, W.A.1    Konnert, J.H.2
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119, 1991.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 84988129057 scopus 로고
    • Optimization of parameters from semiempirical methods. I. Method
    • Stewart, J.J.P. Optimization of parameters from semiempirical methods. I. Method. J. Comput. Chem. 10:209-217, 1989.
    • (1989) J. Comput. Chem. , vol.10 , pp. 209-217
    • Stewart, J.J.P.1
  • 36
    • 0342368473 scopus 로고
    • Department of Biochemistry and Molecular Biophysics. New York: Columbia University
    • Sharp, K.A., Nicholls, A. Program DelPhi, Department of Biochemistry and Molecular Biophysics. New York: Columbia University, 1989.
    • (1989) Program DelPhi
    • Sharp, K.A.1    Nicholls, A.2
  • 37
    • 0000887615 scopus 로고
    • What factors determine cation co-ordination numbers?
    • Brown, I.D. What factors determine cation co-ordination numbers? Acta Crystallogr. 644:545-553, 1979.
    • (1979) Acta Crystallogr. , vol.644 , pp. 545-553
    • Brown, I.D.1
  • 40
    • 0028913979 scopus 로고
    • Wild-type and mutant D-xylose isomerase from Actinoplanes missouriensis: Metal-ion dissociation constants, kinetic parameters of deuterated and non-deuterated substrates and solvent-isotope effects
    • Van Bastelaere, P.B.M., Kersters-Hilderson, H.L.M., Lambeir, A.M. Wild-type and mutant D-xylose isomerase from Actinoplanes missouriensis: Metal-ion dissociation constants, kinetic parameters of deuterated and non-deuterated substrates and solvent-isotope effects. Biochem. J. 307:135-142, 1995.
    • (1995) Biochem. J. , vol.307 , pp. 135-142
    • Van Bastelaere, P.B.M.1    Kersters-Hilderson, H.L.M.2    Lambeir, A.M.3
  • 43
    • 0010717831 scopus 로고
    • TRIPOS Associates, St. Louis, MO
    • SYBYL Program Version 6.0a (1993) TRIPOS Associates, St. Louis, MO.
    • (1993) SYBYL Program Version 6.0a


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.