Divergence of Catalytic Mechanism within a Glycosidase Family Provides Insight into Evolution of Carbohydrate Metabolism by Human Gut Flora
暂无分享,去创建一个
[1] R. Sjöholm,et al. Complete assignments of the (1)H and (13)C chemical shifts and J(H,H) coupling constants in NMR spectra of D-glucopyranose and all D-glucopyranosyl-D-glucopyranosides. , 2008, Carbohydrate research.
[2] A. Gasbarrini,et al. Bacteroides thetaiotaomicron in the gut: molecular aspects of their interaction. , 2007, Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver.
[3] L. Tailford,et al. Mannose Foraging by Bacteroides thetaiotaomicron , 2007, Journal of Biological Chemistry.
[4] Donald A. Comfort,et al. Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. , 2007, Biochemistry.
[5] S. Bröer,et al. Structure-function relationships of heterodimeric amino acid transporters , 2007, Cell Biochemistry and Biophysics.
[6] M. Fogg,et al. Ligation independent cloning (LIC) as a rapid route to families of recombinant biocatalysts from sequenced prokaryotic genomes. , 2006, Organic & biomolecular chemistry.
[7] B. Henrissat,et al. Recent structural insights into the expanding world of carbohydrate-active enzymes. , 2005, Current opinion in structural biology.
[8] D. G. Naumoff. GH97 is a new family of glycoside hydrolases, which is related to the α-galactosidase superfamily , 2005, BMC Genomics.
[9] F. Studier,et al. Protein production by auto-induction in high density shaking cultures. , 2005, Protein expression and purification.
[10] Wolfram Tempel,et al. Mechanism of Class 1 (Glycosylhydrolase Family 47) α-Mannosidases Involved in N-Glycan Processing and Endoplasmic Reticulum Quality Control* , 2005, Journal of Biological Chemistry.
[11] Bernard Henrissat,et al. Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18 , 2005, The FEBS journal.
[12] K Henrick,et al. Electronic Reprint Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions , 2022 .
[13] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[14] Wayne F Anderson,et al. Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis. , 2004, Structure.
[15] Š. Janeček,et al. Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis. , 2004, European journal of biochemistry.
[16] B. Henrissat,et al. The Three-dimensional Structure of Invertase (β-Fructosidase) from Thermotoga maritima Reveals a Bimodular Arrangement and an Evolutionary Relationship between Retaining and Inverting Glycosidases* , 2004, Journal of Biological Chemistry.
[17] Robert C. Edgar,et al. MUSCLE: multiple sequence alignment with high accuracy and high throughput. , 2004, Nucleic acids research.
[18] L. Comstock,et al. Bacteroides thetaiotaomicron: a dynamic, niche-adapted human symbiont. , 2003, Bioessays.
[19] A. Tanner,et al. Cloning and expression of alpha-D-glucosidase and N-acetyl-beta-glucosaminidase from the periodontal pathogen, Tannerella forsythensis (Bacteroides forsythus). , 2003, Oral microbiology and immunology.
[20] Thomas C. Terwilliger,et al. Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement , 2003, Acta crystallographica. Section D, Biological crystallography.
[21] Z. Fujimoto,et al. Crystal Structure of Rice α-Galactosidase Complexed with D-Galactose* , 2003, Journal of Biological Chemistry.
[22] Lynn K. Carmichael,et al. A Genomic View of the Human-Bacteroides thetaiotaomicron Symbiosis , 2003, Science.
[23] L. Hannick,et al. The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. , 2002, Structure.
[24] A. Salyers,et al. New Regulatory Gene That Contributes to Control ofBacteroides thetaiotaomicron Starch Utilization Genes , 2001, Journal of bacteriology.
[25] B. Matthews,et al. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. , 2001, Biochemistry.
[26] N. Wicker,et al. Secator: a program for inferring protein subfamilies from phylogenetic trees. , 2001, Molecular biology and evolution.
[27] D. Kuntz,et al. Structure of Golgi α‐mannosidase II: a target for inhibition of growth and metastasis of cancer cells , 2001, The EMBO journal.
[28] P. Howell,et al. Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases* , 2000, The Journal of Biological Chemistry.
[29] T. Borchert,et al. Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes. , 2000, Biochemistry.
[30] S. Withers,et al. Glycosidase mechanisms: anatomy of a finely tuned catalyst. , 1999, Accounts of chemical research.
[31] Birte Svensson,et al. Recent Advances in Carbohydrate Bioengineering , 1999 .
[32] Thomas C. Terwilliger,et al. Automated MAD and MIR structure solution , 1999, Acta crystallographica. Section D, Biological crystallography.
[33] Pedro M. Coutinho,et al. Carbohydrate-active enzymes : an integrated database approach , 1999 .
[34] B Henrissat,et al. Structural and sequence-based classification of glycoside hydrolases. , 1997, Current opinion in structural biology.
[35] B. Henrissat,et al. Domain Evolution in the α-Amylase Family , 1997, Journal of Molecular Evolution.
[36] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[37] R M Esnouf,et al. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. , 1997, Journal of molecular graphics & modelling.
[38] O Gascuel,et al. BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. , 1997, Molecular biology and evolution.
[39] A. Salyers,et al. Characterization of four outer membrane proteins that play a role in utilization of starch by Bacteroides thetaiotaomicron , 1997, Journal of bacteriology.
[40] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[41] A. Salyers,et al. Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase to growth of Bacteroides thetaiotaomicron on starch , 1996, Journal of bacteriology.
[42] R. E. Huber,et al. Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Brønsted acid-base catalysis of beta-D-galactopyranosyl group transfer. , 1996, Biochemistry.
[43] B. Matthews,et al. Structure-based design of a lysozyme with altered catalytic activity , 1995, Nature Structural Biology.
[44] S. Withers,et al. Changing Enzymic Reaction Mechanisms by Mutagenesis: Conversion of a Retaining Glucosidase to an Inverting Enzyme , 1994 .
[45] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[46] V S Lamzin,et al. Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.
[47] A. Salyers,et al. Characterization of a neopullulanase and an alpha-glucosidase from Bacteroides thetaiotaomicron 95-1 , 1991, Journal of bacteriology.
[48] T. Selwood,et al. A solvent-isotope-effect study of proton transfer during catalysis by Escherichia coli (lacZ) beta-galactosidase. , 1990, The Biochemical journal.
[49] S. Withers,et al. The necessity of magnesium cation for acid assistance aglycone departure in catalysis by Escherichia coli (lacZ) beta-galactosidase. , 1978, The Biochemical journal.
[50] J. Knowles,et al. The intrinsic pKa-values of functional groups in enzymes: improper deductions from the pH-dependence of steady-state parameters. , 1976, CRC critical reviews in biochemistry.
[51] Daniel E. Koshland,et al. STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS , 1953 .