The volatile compounds that constitute the fruit aroma of ripe tomato
(Solanum lycopersicum) are often sequestered in glycosylated form.
A homology-based screen was used to identify the geneSlUGT5, which is
a member of UDP-glycosyltransferase 72 family and shows specificity
towards a range of substrates, including flavonoid, flavanols, hydroqui-none, xenobiotics and chlorinated pollutants.
The dihydrochalcone phlorizin (phloretin 2¢-glucoside) contributes to the
flavor, color and health benefits of apple fruit and processed products. A
genomics approach was used to identify the geneMdPGT1in apple (Ma-lus x domestica) with homology to the UDP-glycosyltransferase 88 family
of uridine diphosphate glycosyltransferases that show specificity towards
The glycosyltransferase enzymes (Lgts) responsible for the biosynthesis of
the lipooligosaccharide-derived oligosaccharide structures from Moraxella
catarrhalishave been investigated. This upper respiratory tract pathogen is
responsible for a spectrum of illnesses, including otitis media (middle ear
infection) in children, and contributes to exacerbations of chronic obstruct-ive pulmonary disease in elderly patients.
Cyclodextrin glycosyltransferase catalyzes the formation of a mixture of
cyclodextrins from starch by an intramolecular transglycosylation reaction.
To manipulate the product specificity of thePaenibacillussp. A11 and
Bacillus maceranscyclodextrin glycosyltransferases towards the preferential
formation of c-cyclodextrin (CD8), crosslinked imprinted proteins of both
cyclodextrin glycosyltransferases were prepared by applying enzyme
imprinting and immobilization methodologies.
Cyclodextrin glycosyltransferase (CGTase) uses ana-retain-ingdoubledisplacementmechanismtocatalyze threedistinct
transglycosylation reactions. To investigate these reactions
as catalyzed by the CGTase fromThermoanaerobacterium
thermosulfurigenesthe enzyme was overproduced (8 mgÆL
culture) usingBacillus subtilisas a host. Detailed analysis
revealed that the three reactions proceed via different kinetic
The plant enzyme arbutin synthase isolated from cell sus-pension cultures ofRauvolfia serpentinaand heterologously
expressed inEscherichia coliis a member of the NRD1b
family of glycosyltransferases. This enzyme was used to
prove, by site-directed mutagenesis, suggested catalytic
domains and reaction mechanisms proposed for enzyme-catalyzed glycosylation. Replacement of amino acids far
from the NRD domain do not significantly affect arbutin
Theb1,3-glycosyltransferase enzymes identi®ed to date
share several conserved regions and conserved cysteine res-idues, all being located in the putative catalytic domain. To
investigate the importance of these motifs and cysteines for
the enzymatic activity, 14 mutants of the murine b1,3-galactosyltransferase-I gene were constructed and expressed
in Sf9 insect cells. Seven mutations abolished the galacto-syltransferase activity.
Nhóm máu di truyền từ cả cha lẫn mẹ. Type nhóm máu ABO được kiểm soát bởi một gene đơn độc có 3 alleles (gen đẳng vị): i, IA, và IB.
H1-Các alleles ABO di truyền từ cha mẹ, và kiểu gen (genotype) ABO ở con Gen đơn độc này mã hoá một enzyme glycosyltransferase—là enzyme làm biến đổi lượng carbohydrate của các antigens trong hồng cầu.
H2-Cấu trúc hồng cầu thuộc các nhóm máu O, A, B và AB khác nhau Gene này khu trú trên nhánh dài của nhiễm sắc thể thứ 9 (9q34). Allele IA cho ra nhóm...
Leukocyte rolling is an important step for the successful recruitment of leu-kocytes into tissue and occurs predominantly in inflamed microvessels and
in high endothelial venules of secondary lymphoid organs. Leukocyte roll-ing is mediated by a group of C-type lectins, termed selectins. Three differ-ent selectins have been identified – P-, E- and L-selectin – which recognize
and bind to crucial carbohydrate determinants on selectin ligands.
Cell wall biosynthesis is a key target for antibacterial drugs. The major
constituent of the bacterial wall, peptidoglycan, is a netlike polymer
responsible for the size and shape of the cell and for resisting osmotic pres-sure. It consists of glycan chains of repeating disaccharide units cross-linked through short peptide chains.
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc
transferases), which initiate mucin-type O-glycan biosynthesis, have broad
acceptor substrate specificities, and it is still unclear how they recognize
peptides with different sequences.
Saccharomyces cerevisiaeGpi3p is the UDP-GlcNAc-bind-ing andpresumed catalytic subunit of the enzyme that forms
GlcNAc-phosphatidylinositol in glycosylphosphatidylinosi-tol biosynthesis. It is anessential proteinwithanEX7
that is conserved in four families of retaining glycosyl-transferases. All Gpi3ps contain a cysteine residue four
residues C-terminal to EX7E. To test their importance for
Gpi3p functionin vivo,Glu289 and297 in theEX7