BIOPEP-UWM: Report

ID 3238
Name Bombolitin I precursor
sequence
IKITTMLAKLGKVLAHVG
Function:
Precursor of hemolytic peptide
 
Number of residues
18
Activity code
he
Activity :
haemolytic
Chemical mass 1893.3788 Monoisotopic mass 1892.1609
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@@](C)(NC(=O)[C@]([H])(CC(C)C)NC(=O)[C@]([H])(CCSC)NC(=O)[C@@]([H])(NC(=O)[C@@]([H])(NC(=O)[C@@]([H])(NC(=O)[C@]([H])(CCCCN)NC(=O)[C@@]([H])(N)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)O)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/C87H157N23O21S/c1-20-49(13)66(91)82(126)100-58(30-24-27-34-90)78(122)108-69(50(14)21-2)85(129)109-71(54(18)112)87(131)110-70(53(17)111)86(130)101-59(31-35-132-19)76(120)104-61(37-45(5)6)79(123)96-51(15)72(116)99-57(29-23-26-33-89)75(119)103-60(36-44(3)4)74(118)93-41-64(113)98-56(28-22-25-32-88)77(121)107-68(48(11)12)84(128)105-62(38-46(7)8)80(124)97-52(16)73(117)102-63(39-55-40-92-43-95-55)81(125)106-67(47(9)10)83(127)94-42-65(114)115/h40,43-54,56-63,66-71,111-112H,20-39,41-42,88-91H2,1-19H3,(H,92,95)(H,93,118)(H,94,127)(H,96,123)(H,97,124)(H,98,113)(H,99,116)(H,100,126)(H,101,130)(H,102,117)(H,103,119)(H,104,120)(H,105,128)(H,106,125)(H,107,121)(H,108,122)(H,109,129)(H,110,131)(H,114,115)/t49-,50-,51-,52-,53+,54+,56-,57-,58-,59-,60-,61-,62-,63-,66-,67-,68-,69-,70-,71-/m0/s1

InChIKey=GZPNOKQHPPJYNG-TZBIIREHSA-N


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

Peptide is the precursor of Bombolitin I (ID 3239 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: