Results 11 to 20 of about 2,313 (194)

Molecular Phylogeny and Predicted 3D Structure of Plant beta-D-N-Acetylhexosaminidase [PDF]

The Scientific World Journal, 2014
beta-D-N-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal of β-1,4-linked N-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree of β-hexosaminidases to analyze the evolutionary
Md. Anowar Hossain, Hairul Azman Roslan
doaj   +3 more sources

Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans. [PDF]

Microb Cell Fact, 2021
Background Sulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation.
Chuzel L, Fossa SL, Boisvert ML, Cajic S, Hennig R, Ganatra MB, Reichl U, Rapp E, Taron CH.   +8 more
europepmc   +3 more sources

Bicistronic lentiviral vector corrects β-hexosaminidase deficiency in transduced and cross-corrected human Sandhoff fibroblasts

Neurobiology of Disease, 2005
Sandhoff disease is an autosomal recessive neurodegenerative disease characterized by a GM2 ganglioside intralysosomal accumulation. It is due to mutations in the β-hexosaminidases β-chain gene, resulting in a β-hexosaminidases A (αβ) and B (ββ ...
Audrey Arfi, Christophe Bourgoin, Luisa Basso, Carla Emiliani, Brunella Tancini, Vanna Chigorno, Yu-Teh Li, Aldo Orlacchio, Livia Poenaru, Sandro Sonnino, Catherine Caillaud   +10 more
doaj   +1 more source

Síntese de inibidores potenciais de hexosaminidases derivados de N-acetilglicosamina e D-glicose

Orbital: The Electronic Journal of Chemistry, 2012
We report herein the synthesis and characterization of N-acetylglucosamine and D-glucose derivates modified at C-1 for evaluation of antifungal activity as potential hexosaminidases inhibitors.
Lucas Lopardi Franco, Mário C. Brandão, Ricardo José Alves, José Dias Souza Filho   +3 more
doaj   +1 more source

Characterization of recombinant human lysosomal beta-hexosaminidases produced in the methylotrophic yeast Pichia pastoris

Universitas Scientiarum, 2016
β-hexosaminidases (Hex) are dimeric enzymes involved in the lysosomal degradation of glycolipids and glycans. They are formed by α- and/or β-subunits encoded byHEXA and HEXB genes, respectively.
Angela Johana Espejo Mojica, Angela Rocío Mosquera, Edwin Alexander Rodríguez-López, Dennis Johana Díaz, Laura Milena Betrán, Francy Liliana Hernández, Carlos Javier Alméciga Díaz, Luis Alejandro Barrera   +7 more
doaj   +1 more source

Induced secretion of β-hexosaminidase by human brain endothelial cells: A novel approach in Sandhoff disease?

Neurobiology of Disease, 2010
Sandhoff disease is an autosomal recessive lysosomal disorder due to mutations in the β-hexosaminidase β-chain gene, resulting in β-hexosaminidases A (αβ) and B (ββ) deficiency and GM2 ganglioside accumulation in the brain.
Lionel Batista, Florence Miller, Céline Clave, Audrey Arfi, Gaëlle Douillard-Guilloux, Pierre-Olivier Couraud, Catherine Caillaud   +6 more
doaj   +1 more source

Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster. [PDF]

PLoS Genetics, 2014
As newly synthesized glycoproteins move through the secretory pathway, the asparagine-linked glycan (N-glycan) undergoes extensive modifications involving the sequential removal and addition of sugar residues.
Erica E Rosenbaum, Eva Vasiljevic, Kimberley S Brehm, Nansi Jo Colley   +3 more
doaj   +1 more source

O-GlcNAcase:promiscuous hexosaminidase or key regulator of O-GlcNAc signalling? [PDF]

, 2014
O-GlcNAc signaling is regulated by an opposing pair of enzymes: O-GlcNAc transferase installs and O-GlcNAcase (OGA) removes the modification from proteins.
Banerjee, Butkinaree, Cantarel, Cecioni, Cetinba, Comtesse, Copeland, Dennis, Dong, Dorfmueller, Dorfmueller, Drougat, Forsythe, Francisco, Gao, Gong, Graham, Guinez, Hanover, Hart, Hayakawa, He, He, Heckel, Hilgers, Housley, Howerton, Hu, Itkonen, Keembiyehetty, Knapp, Laczy, Lefebvre, Lepage, Libina, Liu, Macauley, Macauley, Macauley, Macauley, Macauley, Mahuran, Martin, Minami, Müller, Nagel, Olszewski, Ostrowski, Pathak, Penton, Radermacher, Rahman, Rao, Rao, Robinson, Ruan, Ruan, Schimpl, Schimpl, Schultz, Sekine, Shen, Slawson, Speakman, Stryke, Swallow, Tews, Toleman, Toleman, Torres, Wang, Wang, Webster, Wells, Whisenhunt, Whitworth, Yang, Yu, Yuzwa, Yuzwa, Zachara, Zachara, Zhu   +82 more
core   +3 more sources

Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate [PDF]

, 2001
Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques(1). A catalytic mechanism, featuring a long-lived oxo-carbenium-ion intermediate, was proposed on the basis of model ...
A Federov, AL Fink, AT Brünger, BA Malcolm, BL Mark, CC Blake, Collaborative Computational Project Number 4, DC Phillips, DE Koshland, DM Chipman, E Holler, FW Ballardie, FW Dahlquist, G Sulzenbacher, GJ Davies, GJ Davies, GN Murshodov, I Matsumura, I Tews, ML Sinnott, NCJ Strynadka, Q Wang, R Kuroki, S Rosenberg, T Rand-Meir, TL Amyes, V Notenboom, WP Burmeister, Z Otwinowski   +28 more
core   +1 more source

A single site in human β-hexosaminidase A binds both 6-sulfate-groups on hexosamines and the sialic acid moiety of GM2 ganglioside [PDF]

, 2003
Human β-hexosaminidase A (Hex A) (αβ) is composed of two subunits whose primary structures are ∼60% identical. Deficiency of either subunit results in severe neurological disease due to the storage of GM2 ganglioside; Tay–Sachs disease, α deficiency, and
Abbink, E.J., Beulens, J.W., Dekker, J.M., Dekkers, O.M., DeVries, J.H., Diabet Pearl Parelsnoer Initiative, Elders, P.J.M., Holleman, F., Nijpels, G., Ozcan, B., Pijl, H., Rauh, S.P., Rutte, A., Rutters, F., Schaper, N.C., Schram, M.T., Sijbrands, E.J.G., Silvius, B., Stehouwer, C.D.A., Tack, C.J., Valk, H.W. de, Wolffenbuttel, B.H.R.   +21 more
core   +11 more sources