scholarly journals α-Klotho Induces FGF23-derived Signal as a Scaffold Molecule Without Glycosidase Activity

2018 ◽  
Vol 30 (176) ◽  
pp. J151-J152
Author(s):  
Jyoji Morise
Keyword(s):  
Glycosidase Activity ◽  
Scaffold Molecule

Sensitive and rapid electrochemical bioassay of glycosidase activity

The Analyst ◽  
2006 ◽  
Vol 131 (8) ◽  
pp. 889 ◽  
Author(s):  
Tanin Tangkuaram ◽  
Jared Q. Gerlach ◽  
Yun Xiang ◽  
Abdel-Nasser Kawde ◽  
Zong Dai ◽  
...  
Keyword(s):  
Glycosidase Activity ◽  
Electrochemical Bioassay

scholarly journals Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Gloria Gamiz-Arco ◽  
Luis I. Gutierrez-Rus ◽  
Valeria A. Risso ◽  
Beatriz Ibarra-Molero ◽  
Yosuke Hoshino ◽  
...  
Keyword(s):  
Sequence Space ◽  
Conformational Flexibility ◽  
Allosteric Modulation ◽  
Heme Binding ◽  
Optimum Temperature ◽  
Glycosidic Bonds ◽  
Glycosidase Activity ◽  
Tim Barrel ◽  
Crystallographic Structures ◽  
Ancestral Protein

AbstractGlycosidases are phylogenetically widely distributed enzymes that are crucial for the cleavage of glycosidic bonds. Here, we present the exceptional properties of a putative ancestor of bacterial and eukaryotic family-1 glycosidases. The ancestral protein shares the TIM-barrel fold with its modern descendants but displays large regions with greatly enhanced conformational flexibility. Yet, the barrel core remains comparatively rigid and the ancestral glycosidase activity is stable, with an optimum temperature within the experimental range for thermophilic family-1 glycosidases. None of the ∼5500 reported crystallographic structures of ∼1400 modern glycosidases show a bound porphyrin. Remarkably, the ancestral glycosidase binds heme tightly and stoichiometrically at a well-defined buried site. Heme binding rigidifies this TIM-barrel and allosterically enhances catalysis. Our work demonstrates the capability of ancestral protein reconstructions to reveal valuable but unexpected biomolecular features when sampling distant sequence space. The potential of the ancestral glycosidase as a scaffold for custom catalysis and biosensor engineering is discussed.

Role of TYR70 in the N-glycosidase activity of neo-trichosanthin

Toxicon ◽  
1999 ◽  
Vol 37 (7) ◽  
pp. 961-972 ◽  
Author(s):  
Li Yan ◽  
Shen Wu ◽  
Hui-Guang Li ◽  
Jian-Hui Li ◽  
R.N.-S Wong ◽  
...  
Keyword(s):  
Glycosidase Activity

The synthesis of a decapeptide with glycosidase activity

1973 ◽  
Vol 29 (7) ◽  
pp. 786-788 ◽  
Author(s):  
P. K. Chakravarty ◽  
K. B. Mathur ◽  
M. M. Dhar
Keyword(s):  
Glycosidase Activity

scholarly journals Polynucleotide: adenosine glycosidase activity of saporin-L1: effect on DNA, RNA and poly(A)

1996 ◽  
Vol 319 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Luigi BARBIERI ◽  
Paola VALBONESI ◽  
Paola GORINI ◽  
Annalisa PESSION ◽  
Fiorenzo STIRPE
Keyword(s):  
Ionic Strength ◽  
Kinetic Parameters ◽  
Plant Protein ◽  
Ribosome Inactivating Proteins ◽  
Glycosidase Activity ◽  
Plant Enzymes ◽  
Low Ionic Strength ◽  
Different Sources ◽  
Saponaria Officinalis ◽  
Optimal Ph

The ribosome-inactivating proteins (RIPs) are a family of plant enzymes for which a unique activity has been determined: rRNA N-glycosidase, which removes adenine at a specific universally conserved position (A4324 in the case of rat ribosomes). Here we report that saporin-L1, a RIP from the leaves of Saponaria officinalis, recognizes other substrates, including RNAs from different sources, DNA and poly(A). Saporin-L1 depurinated DNA extensively and released adenine from all adenine-containing polynucleotides tested. Adenine was the only base released from DNA or artificial polynucleotides. The characteristics of the reactions catalysed by saporin-L1 have been determined: optimal pH and temperature, ionic requirements, and the kinetic parameters Km and kcat. The reaction proceeded without cofactors, at low ionic strength, in the absence of Mg2+ and K+. Saporin-L1 had no activity towards various adenine-containing non-polynucleotide compounds (cytokinins, cofactors, nucleotides). This plant protein may now be classified as a polynucleotide:adenosine glycosidase.

Glycosidases in Normal Human Leukocytes and Abnormalities in GM1-Gangliosidosis

1972 ◽  
Vol 18 (9) ◽  
pp. 971-975 ◽  
Author(s):  
Jeffrey Hindman ◽  
Edward Cotlier
Keyword(s):  
Enzyme Assay ◽  
Large Population ◽  
Genetic Defect ◽  
Normal Subjects ◽  
Confidence Limits ◽  
Gm1 Gangliosidosis ◽  
Glycosidase Activity ◽  
Normal Ranges ◽  
Normal Human ◽  
Single Enzyme

Abstract Leukocyte enzyme assay is a valuable tool in the diagnosis of mucolipidoses and glycosphingolipidoses. Accurate resolution of the normal ranges of glycosidase activity is vital in the evaluation of both homozygotes and suspected heterozygote carriers. Activities of leukocyte β-galactosidase, α-galactosidase, α-mannosidase, β-fucosidase, β-glucosaminidase, and β-galactosaminidase were measured in a large population of normal subjects and demonstrated, within 95% confidence limits, to be normally distributed. Leukocyte glycosidases were determined in a GM1-gangliosidosis homozygote and in the heterozygous parents. A previously unreported deficiency of β-fucosidase and the well-known deficiency of β-galactosidase were demonstrated in the proband, and corresponding but less severe deficiencies of both glycosidases were found in the parents. β-Galactosidase and β-fucosidase may represent a single enzyme, unspecific for the carbon 6 of galactose. If not, the genetic defect in GM1-gangliosidosis may be more profound than has been recognized.

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