THE ROLE OF THE HYDROXY AMINO ACID IN THE TRIPLET SEQUENCE ASN-X-SER/THR FOR N-GLYCOSYLATION

1981 ◽  
Vol 9 (2) ◽  
pp. 143P-143P
Author(s):  
Ernst Bause ◽  
Günter Legler
Keyword(s):  
Amino Acid ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

scholarly journals The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis

1981 ◽  
Vol 195 (3) ◽  
pp. 639-644 ◽  
Author(s):  
E Bause ◽  
G Legler
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Hydroxy Group ◽  
Catalytic Mechanism ◽  
Hydrogen Bond Donor ◽  
Hydrogen Bond Interaction ◽  
Hydrogen Bond Acceptor ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

The catalytical role of the hydroxy amino acid in the “marker sequence” Asn-Xaa-Thr(Ser) for the N-glycosylation step of glycoprotein formation was investigated by using a series of hexapeptides derived from Tyr-Asn-Gly-Xaa-Ser-Val by substituting threonine, serine, cysteine, valine and O-methylthreonine respectively for Xaa. The results, which were obtained with calf liver microsomal fractions as enzyme source and dolichyl diphosphate di-N-acetyl [14C] chitobiose as glycosyl donor showed that the threonine-, serine- and cysteine-containing derivatives could be glycosylated, although at very different rates, whereas the valine and O-methylthreonine analogues did not work as glycosyl acceptors. Replacement of threonine by serine resulted in a 4-fold decrease in Vmax, and about a 10-fold increase in Km for glycosyl transfer. Replacement of serine by cysteine again decreased acceptor activity 2-3-fold. The various results, taken together, indicate an absolute requirement for a hydrogen-bond-donor function in the side chain of the hydroxy amino acid of the “marker sequence” and furthermore, point to a considerable influence of the structure of this amino acid on binding as well as on the glycosyl transfer itself. In order to explain the observed differences in the glycosyl-transfer rates, a model is proposed with a hydrogen-bond interaction between the amide of asparagine as the hydrogen-bond donor and the oxygen of the hydroxy group of the hydroxy amino acid as the hydrogen-bond acceptor. The participation of the hydroxy group in the catalytic mechanism of glycosyl transfer in the kind of proton-relay system is discussed.

Depsipeptides Communication 31. Synthesis of depsipeptides containing ?-hydroxy ?-amino acid residues

1965 ◽  
Vol 14 (11) ◽  
pp. 1954-1957
Author(s):  
G. A. Ravdel' ◽  
N. A. Krit ◽  
V. A. Oladkina ◽  
L. A. Shchukina ◽  
M. M. Shemyakin
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

scholarly journals Concise and Straightforward Asymmetric Synthesis of a Cyclic Natural Hydroxy-Amino Acid

Molecules ◽  
2014 ◽  
Vol 19 (12) ◽  
pp. 19516-19531 ◽  
Author(s):  
Mario Simirgiotis ◽  
Javier Vallejos ◽  
Carlos Areche ◽  
Beatriz Sepúlveda
Keyword(s):  
Amino Acid ◽  
Asymmetric Synthesis ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

D-Threonine Aldolase and Its Application to D -β-Hydroxy-£-Amino Acid Synthesis

1992 ◽  
pp. 96-99
Author(s):  
Masahisa Ikemi ◽  
Tadashi Morikawa ◽  
Teruzo Miyoshi ◽  
Sakayu Shimizu ◽  
Michihiko Kataoka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Hydroxy Amino Acid ◽  
Threonine Aldolase ◽  
Hydroxy Amino
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