Amino acid sequence of .kappa.-flavitoxin: establishment of a new family of snake venom neurotoxins

Biochemistry ◽  
1988 ◽  
Vol 27 (10) ◽  
pp. 3794-3798 ◽  
Author(s):  
Gregory A. Grant ◽  
Mark W. Frazier ◽  
Vincent A. Chiappinelli
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom ◽  
New Family

Amino acid sequence of a snake venom toxin that binds to the muscarinic acetylcholine receptor

Toxicon ◽  
1991 ◽  
Vol 29 (4-5) ◽  
pp. 521-526 ◽  
Author(s):  
Evert Karlsson ◽  
Carl Risinger ◽  
Mikael Jolkkonen ◽  
Christer Wernstedt ◽  
Abdu Adem
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetylcholine Receptor ◽  
Snake Venom ◽  
Muscarinic Acetylcholine Receptor ◽  
Muscarinic Acetylcholine ◽  
Venom Toxin ◽  
Snake Venom Toxin

Amino acid sequence of piratoxin-I, a myotoxin fromBothrops pirajai snake venom, and its biological activity after alkylation withp-bromophenacyl bromide

1998 ◽  
Vol 17 (7) ◽  
pp. 713-718 ◽  
Author(s):  
Marcos H. Toyama ◽  
Andreimar M. Soares ◽  
Carlos A. Vieira ◽  
José C. Novello ◽  
Benedito Oliveira ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom

scholarly journals Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities

2009 ◽  
Vol 12 (10) ◽  
pp. 2273-2281 ◽  
Author(s):  
Leandra Watanabe ◽  
John D. Shannon ◽  
Richard H. Valente ◽  
Alexandra Rucavado ◽  
Alberto Alape-Girón ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom ◽  
Bothrops Asper

scholarly journals Peptidase E, a Peptidase Specific for N-Terminal Aspartic Dipeptides, Is a Serine Hydrolase

2000 ◽  
Vol 182 (9) ◽  
pp. 2536-2543 ◽  
Author(s):  
Rachel A. L. Lassy ◽  
Charles G. Miller
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Serine Hydrolase ◽  
Genome Sequences ◽  
New Family ◽  
The Family ◽  
Serovar Typhimurium ◽  
Structural Classes

ABSTRACT Salmonella enterica serovar Typhimurium peptidase E (PepE) is an N-terminal Asp-specific dipeptidase. PepE is not inhibited by any of the classical peptidase inhibitors, and its amino acid sequence does not place it in any of the known peptidase structural classes. A comparison of the amino acid sequence of PepE with a number of related sequences has allowed us to define the amino acid residues that are strongly conserved in this family. To ensure the validity of this comparison, we have expressed one of the most distantly related relatives (Xenopus) in Escherichia coli and have shown that it is indeed an Asp-specific dipeptidase with properties very similar to those of serovar Typhimurium PepE. The sequence comparison suggests that PepE is a serine hydrolase. We have used site-directed mutagenesis to change all of the conserved Ser, His, and Asp residues and have found that Ser120, His157, and Asp135 are all required for activity. Conversion of Ser120 to Cys leads to severely reduced (104-fold) but still detectable activity, and this activity but not that of the parent is inhibited by thiol reagents; these results confirm that this residue is likely to be the catalytic nucleophile. These results suggest that PepE is the prototype of a new family of serine peptidases. The phylogenetic distribution of the family is unusual, since representatives are found in eubacteria, an insect (Drosophila), and a vertebrate (Xenopus) but not in the Archaea or in any of the other eukaryotes for which genome sequences are available.

Amino acid sequence and characterization of C-type lectin purified from the snake venom of Crotalus ruber

2007 ◽  
Vol 146 (3) ◽  
pp. 299-306 ◽  
Author(s):  
Jiharu Hamako ◽  
Yukiyo Suzuki ◽  
Nobuhiro Hayashi ◽  
Mina Kimura ◽  
Yasuhiro Ozeki ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom
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