The Classification of Twenty Common Amino Acid Residues in Protected Peptides by Theirβ-Sheet-Structure-Stabilizing Potentials, SPβ, and Its Application to Peptide Synthesis

1993 ◽  
Vol 66 (2) ◽  
pp. 483-488 ◽  
Author(s):  
Mitsuaki Narita ◽  
Jin-Shik Lee ◽  
Yuka Murakawa ◽  
Yoshihisa Kojima
1989 ◽  
Vol 62 (3) ◽  
pp. 773-779 ◽  
Author(s):  
Mitsuaki Narita ◽  
Shizuko Isokawa ◽  
Shinya Honda ◽  
Hiroshi Umeyama ◽  
Hideaki Kakei ◽  
...  

2006 ◽  
Vol 284 (6) ◽  
pp. 575-585 ◽  
Author(s):  
Ivan M. Okhapkin ◽  
Andrei A. Askadskii ◽  
Vladimir A. Markov ◽  
Elena E. Makhaeva ◽  
Alexei R. Khokhlov

1996 ◽  
Vol 318 (1) ◽  
pp. 133-138 ◽  
Author(s):  
Roberto A GEREMIA ◽  
E Alejandro PETRONI ◽  
Luis IELPI ◽  
Bernard HENRISSAT

A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using current alignment algorithms as well as hydrophobic cluster analysis (HCA). These sequences show a similarity which is significant but too low to be reliably aligned using automatic alignment methods. However, a region spanning approx. 270 residues in these proteins could be aligned by HCA, and several invariant amino acid residues were identified. These features were also found in several other glycosyltransferases, as well as in proteins of unknown function present in sequence databases. This similarity most probably reflects the existence of a family of proteins with conserved structural and mechanistic features. It is argued that the present IUBMB classification of glycosyltransferases could be complemented by a classification of these enzymes based on sequence similarities analogous to that which we proposed for glycosyl hydrolases [Henrissat, B. (1991) Biochem. J. 280, 309–316].


2011 ◽  
Vol 30 (4) ◽  
pp. 290-297
Author(s):  
Michio Asada ◽  
Hideki Hirakawa ◽  
Satoru Kuhara

2015 ◽  
Vol 21 (6) ◽  
pp. 454-460 ◽  
Author(s):  
Keiko Masuda ◽  
Haruka Ooyama ◽  
Kenshiro Shikano ◽  
Kunihiro Kondo ◽  
Megumi Furumitsu ◽  
...  

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