BIOPEP-UWM: Report

ID 3236
Name Bombolitin II precursor
sequence
SKITDILAKLGKVLAHVG
Function:
Precursor of hemolytic peptide
 
Number of residues
18
Activity code
he
Activity :
haemolytic
Chemical mass 1863.2427 Monoisotopic mass 1862.1318
EC50 :
0.00 µM


Bibliographic data:
Authors
Argiolas A., Pisano J. J.
Title
Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. J. Biol. Chem., 260, 1437-1444, 1985
Year Source
1985 Journal


Additional information:
BIOPEP-UWM database of bioactive peptides

SMILES: [H][C@](N)(CO)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@@H](C)CC)C(=O)N[C@@]([H])([C@@H](C)O)C(=O)N[C@@]([H])(CC(O)=O)C(=O)N[C@@]([H])([C@@H](C)CC)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC1=CN=CN1)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(O)=O

InChI=1S/C85H151N23O23/c1-18-47(13)67(107-80(126)61(36-63(112)113)103-85(131)69(51(17)110)108-84(130)68(48(14)19-2)106-76(122)56(28-22-25-31-88)98-72(118)53(89)40-109)83(129)102-59(34-44(7)8)78(124)94-49(15)70(116)97-55(27-21-24-30-87)74(120)100-57(32-42(3)4)73(119)91-38-62(111)96-54(26-20-23-29-86)75(121)105-66(46(11)12)82(128)101-58(33-43(5)6)77(123)95-50(16)71(117)99-60(35-52-37-90-41-93-52)79(125)104-65(45(9)10)81(127)92-39-64(114)115/h37,41-51,53-61,65-69,109-110H,18-36,38-40,86-89H2,1-17H3,(H,90,93)(H,91,119)(H,92,127)(H,94,124)(H,95,123)(H,96,111)(H,97,116)(H,98,118)(H,99,117)(H,100,120)(H,101,128)(H,102,129)(H,103,131)(H,104,125)(H,105,121)(H,106,122)(H,107,126)(H,108,130)(H,112,113)(H,114,115)/t47-,48-,49-,50-,51+,53-,54-,55-,56-,57-,58-,59-,60-,61-,65-,66-,67-,68-,69-/m0/s1

InChIKey=YTQVXZZCGXKRIR-PRFBEJPASA-N


The active form is C-terminal amide group instead of C-terminal glycine residue.

Peptide is the precursor of Bombolitin II (ID 3237 in BIOPEP-UWM database of bioactive peptides).

Reviews concerning C-terminal amidation of peptides:

Bradbury A. F., Smyth D. G., 1991, Peptide amidation. Trends Biochem. Sci., 16, 112-115

Merkler D. J., 1994, C-terminal amidated peptides: production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity. Enzyme Microb. Technol., 16, 450-456


Database reference: