scholarly article | Q13442814 |
P356 | DOI | 10.1046/J.1432-1327.2000.01562.X |
P8608 | Fatcat ID | release_3r233n5qgnebxfnjui73pi2hym |
P698 | PubMed publication ID | 10931188 |
P5875 | ResearchGate publication ID | 12389808 |
P50 | author | Paul Kosma | Q41464649 |
P2093 | author name string | B Nidetzky | |
A Reiter | |||
I Petzelbauer | |||
B Splechtna | |||
P2860 | cites work | Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability | Q27743453 |
Nomenclature for sugar-binding subsites in glycosyl hydrolases | Q29618485 | ||
The family 1 beta-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism | Q30432266 | ||
The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction | Q30464699 | ||
Mutagenesis of glycosidases | Q33953576 | ||
Preparation of oligosaccharide units library and its utilization | Q36876209 | ||
Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 1. Brønsted parameters for cleavage of alkyl beta-D-galactopyranosides | Q38291412 | ||
A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactose | Q39092789 | ||
Formation of oligosaccharides from lactose by Bacillus circulans beta-galactosidase | Q39110971 | ||
Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli | Q39839495 | ||
The enhancement of enzymatic rate accelerations by Brønsted acid-base catalysis | Q41747002 | ||
The effect of methanol and dioxan on the rates of the β-galactosidase-catalysed hydrolyses of some β-d-galactopyranosides: rate-limiting degalactosylation. The pH-dependence of galactosylation and degalactosylation | Q41825362 | ||
Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties | Q43017516 | ||
Substrate inhibition or activation kinetics of the beta-galactosidase from the extreme thermoacidophile archaebacterium Caldariella acidophila | Q43017610 | ||
Identification of two glutamic acid residues essential for catalysis in the beta-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus | Q43024429 | ||
beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: structure and activity in the presence of alcohols | Q43026768 | ||
Two-dimensional mapping of N-glycosidically linked asialo-oligosaccharides from glycoproteins as reductively pyridylaminated derivatives using dual separation modes of high-performance capillary electrophoresis. | Q52415093 | ||
Partition analysis and concept of net rate constants as tools in enzyme kinetics | Q52872618 | ||
Catalytic mechanism of enzymic glycosyl transfer | Q53999762 | ||
A capillary electrophoretic study on the specificity of beta-galactosidases from Aspergillus oryzae, Escherichia coli, Streptococcus pneumoniae, and Canavalia ensiformis (jack bean). | Q54570245 | ||
Expression and extensive characterization of a beta-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus in Escherichia coli: authenticity of the recombinant enzyme. | Q54600891 | ||
Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 2. Reactions of the galactosyl-enzyme intermediate with alcohols and azide ion. | Q54603769 | ||
beta-Galactosidases of Escherichia coli with substitutions for Glu-461 can be activated by nucleophiles and can form beta-D-galactosyl adducts. | Q54646677 | ||
P433 | issue | 16 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Sulfolobus solfataricus | Q3503466 |
Pyrococcus furiosus | Q146310 | ||
P304 | page(s) | 5055-5066 | |
P577 | publication date | 2000-08-01 | |
P1433 | published in | FEBS Journal | Q1388041 |
P1476 | title | Transgalactosylation by thermostable beta-glycosidases from Pyrococcus furiosus and Sulfolobus solfataricus. Binding interactions of nucleophiles with the galactosylated enzyme intermediate make major contributions to the formation of new beta-glycosides during lactose conversion | |
P478 | volume | 267 |