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Volumn 411, Issue 1, 2008, Pages 181-190

A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis

Author keywords

Glutaminyl cyclase (glutaminyl peptide cyclotransferase, QC); Hydrogen bond network; Proton transfer; Pyroglutamate (pGlu); Site directed mutagenesis; Synchrotron; X ray crystallography

Indexed keywords

GLUTAMINYL CYCLASE (GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE, QC); HYDROGEN-BOND NETWORKS; PYROGLUTAMATE (PGLU); SITE-DIRECTED MUTAGENESIS;

EID: 41649084118     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071073     Document Type: Article
Times cited : (30)

References (36)
  • 1
    • 0032497366 scopus 로고    scopus 로고
    • Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV
    • Van Coillie, E., Proost, P., Van Aelst, I., Struyf, S., Polfliet, M., De Meester, I., Harvey, D. J., Van Damme, J. and Opdenakker, G. (1998) Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV. Biochemistry 37, 12672-12680
    • (1998) Biochemistry , vol.37 , pp. 12672-12680
    • Van Coillie, E.1    Proost, P.2    Van Aelst, I.3    Struyf, S.4    Polfliet, M.5    De Meester, I.6    Harvey, D.J.7    Van Damme, J.8    Opdenakker, G.9
  • 3
    • 0000495632 scopus 로고
    • Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides
    • Fischer, W. H. and Spiess, J. (1987) Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. U.S.A. 84, 3628-3632
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 3628-3632
    • Fischer, W.H.1    Spiess, J.2
  • 5
    • 0025840609 scopus 로고
    • Primary structure and functional expression of a glutaminyl cyclase
    • Pohl, T., Zimmer, M., Mugele, K. and Spiess, J. (1991) Primary structure and functional expression of a glutaminyl cyclase. Proc. Natl. Acad. Sci. U.S.A. 88, 10059-10063
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 10059-10063
    • Pohl, T.1    Zimmer, M.2    Mugele, K.3    Spiess, J.4
  • 6
    • 0027936053 scopus 로고
    • Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase
    • Song, I., Chuang, C. Z. and Bateman, R. C., Jr. (1994) Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J. Mol. Endocrinol. 13, 77-86
    • (1994) J. Mol. Endocrinol , vol.13 , pp. 77-86
    • Song, I.1    Chuang, C.Z.2    Bateman Jr., R.C.3
  • 7
    • 1842636794 scopus 로고    scopus 로고
    • Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions
    • Schilling, S., Hoffmann, T., Manhart, S., Hoffmann, M. and Demuth, H. U. (2004) Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett. 563, 191-196
    • (2004) FEBS Lett , vol.563 , pp. 191-196
    • Schilling, S.1    Hoffmann, T.2    Manhart, S.3    Hoffmann, M.4    Demuth, H.U.5
  • 8
    • 24944521480 scopus 로고    scopus 로고
    • Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
    • Huang, K. F., Liu, Y. L., Cheng, W. J., Ko, T. P. and Wang, A. H. J. (2005) Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proc. Natl. Acad. Sci. U.S.A. 102, 13117-13122
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 13117-13122
    • Huang, K.F.1    Liu, Y.L.2    Cheng, W.J.3    Ko, T.P.4    Wang, A.H.J.5
  • 14
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • Lowther, W. T. and Matthews, B. W. (2002) Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem. Rev. 102, 4581-4607
    • (2002) Chem. Rev , vol.102 , pp. 4581-4607
    • Lowther, W.T.1    Matthews, B.W.2
  • 16
    • 23244450070 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: A single zinc metalloenzyme
    • Huang, K. F., Liu, Y. L. and Wang, A. H. J. (2005) Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: a single zinc metalloenzyme. Protein Expression Purif. 43, 65-72
    • (2005) Protein Expression Purif , vol.43 , pp. 65-72
    • Huang, K.F.1    Liu, Y.L.2    Wang, A.H.J.3
  • 17
    • 0037361122 scopus 로고    scopus 로고
    • Pyroglutamyl-peptidase I: Cloning, sequencing, and characterisation of the recombinant human enzyme
    • Dando, P. M., Fortunato, M., Strand, G. B., Smith, T. S. and Barrett, A. J. (2003) Pyroglutamyl-peptidase I: cloning, sequencing, and characterisation of the recombinant human enzyme. Protein Expression Purif. 28, 111-119
    • (2003) Protein Expression Purif , vol.28 , pp. 111-119
    • Dando, P.M.1    Fortunato, M.2    Strand, G.B.3    Smith, T.S.4    Barrett, A.J.5
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 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. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 22
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G. J. (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 26
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit, E. A. and Bacon, D. J. (1997) Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 27
    • 0348010383 scopus 로고    scopus 로고
    • Identification of human glutaminyl cyclase as a metalloenzyme: Potent inhibition by imidazole derivatives and heterocyclic chelators
    • Schilling, S., Niestroj, A. J., Rahfeld, J. U., Hoffmann, T., Wermann, M., Zunkel, K., Wasternack, C. and Demuth, H. U. (2003) Identification of human glutaminyl cyclase as a metalloenzyme: potent inhibition by imidazole derivatives and heterocyclic chelators. J. Biol. Chem. 278, 49773-49779
    • (2003) J. Biol. Chem , vol.278 , pp. 49773-49779
    • Schilling, S.1    Niestroj, A.J.2    Rahfeld, J.U.3    Hoffmann, T.4    Wermann, M.5    Zunkel, K.6    Wasternack, C.7    Demuth, H.U.8
  • 28
    • 3843081911 scopus 로고    scopus 로고
    • The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica
    • Bzymek, K. P. and Holz, R. C. (2004) The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica. J. Biol. Chem. 279, 31018-31025
    • (2004) J. Biol. Chem , vol.279 , pp. 31018-31025
    • Bzymek, K.P.1    Holz, R.C.2
  • 29
    • 3342995026 scopus 로고    scopus 로고
    • Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus
    • Fundoiano-Hershcovitz, Y., Rabinovitch, L., Langut, Y. Reiland, V. Shoham, G. and Shoham, Y. (2004) Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus. FEBS Lett, 571, 192-196
    • (2004) FEBS Lett , vol.571 , pp. 192-196
    • Fundoiano-Hershcovitz, Y.1    Rabinovitch, L.2    Langut, Y.3    Reiland, V.4    Shoham, G.5    Shoham, Y.6
  • 30
    • 0034778987 scopus 로고    scopus 로고
    • Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    • Northrop, D. B. (2001) Follow the protons: a low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases. Acc. Chem. Res. 34, 790-797
    • (2001) Acc. Chem. Res , vol.34 , pp. 790-797
    • Northrop, D.B.1
  • 31
    • 33845498406 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 protease in situ product complex and observation of a low-barrier hydrogen bond between catalytic aspartates
    • Das, A., Prashar, V., Mahale, S., Serre, L., Ferrer, J. L. and Hosur, M. V. (2006) Crystal structure of HIV-1 protease in situ product complex and observation of a low-barrier hydrogen bond between catalytic aspartates. Proc. Natl. Acad. Sci. U.S.A. 103, 18464-18469
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18464-18469
    • Das, A.1    Prashar, V.2    Mahale, S.3    Serre, L.4    Ferrer, J.L.5    Hosur, M.V.6
  • 32
    • 32344440010 scopus 로고    scopus 로고
    • Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P
    • Jao, S. C., Huang, L. F., Hwang, S. M. and Li, W. S. (2006) Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P. Biochemistry 45, 1547-1553
    • (2006) Biochemistry , vol.45 , pp. 1547-1553
    • Jao, S.C.1    Huang, L.F.2    Hwang, S.M.3    Li, W.S.4
  • 33
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn, B. M. (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102, 4431-4458
    • (2002) Chem. Rev , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 34
    • 34250362770 scopus 로고    scopus 로고
    • Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer: Role of an active site asparagine residue in activation of methyl transfer by methyltransferases
    • Doukov, T. I., Hemmi, H., Drennan, C. L. and Ragsdale, S. W. (2007) Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer: role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J. Biol. Chem. 282, 6609-6618
    • (2007) J. Biol. Chem , vol.282 , pp. 6609-6618
    • Doukov, T.I.1    Hemmi, H.2    Drennan, C.L.3    Ragsdale, S.W.4


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