BIOPEP-UWM: Report

ID 3235
Name Bombolitin III precursor
sequence
IKIMDILAKLGKVLAHVG
Function:
Precursor of hemolytic peptide
 
Number of residues
18
Activity code
he
Activity :
haemolytic
Chemical mass 1919.4160 Monoisotopic mass 1918.1765
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])(NC(=O)[C@]([H])(CC(O)=O)NC(=O)[C@]([H])(CCSC)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)CC)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/C89H159N23O21S/c1-20-51(14)69(93)85(129)102-59(31-25-28-35-92)80(124)111-72(52(15)21-2)88(132)103-60(32-36-134-19)78(122)106-65(41-67(114)115)84(128)112-73(53(16)22-3)89(133)108-63(39-48(8)9)82(126)98-54(17)74(118)101-58(30-24-27-34-91)77(121)105-61(37-46(4)5)76(120)95-43-66(113)100-57(29-23-26-33-90)79(123)110-71(50(12)13)87(131)107-62(38-47(6)7)81(125)99-55(18)75(119)104-64(40-56-42-94-45-97-56)83(127)109-70(49(10)11)86(130)96-44-68(116)117/h42,45-55,57-65,69-73H,20-41,43-44,90-93H2,1-19H3,(H,94,97)(H,95,120)(H,96,130)(H,98,126)(H,99,125)(H,100,113)(H,101,118)(H,102,129)(H,103,132)(H,104,119)(H,105,121)(H,106,122)(H,107,131)(H,108,133)(H,109,127)(H,110,123)(H,111,124)(H,112,128)(H,114,115)(H,116,117)/t51-,52-,53-,54-,55-,57-,58-,59-,60-,61-,62-,63-,64-,65-,69-,70-,71-,72-,73-/m0/s1

InChIKey=LZENTCVJRMLPDX-LRAUCXAHSA-N


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

Peptide is the precursor of Bombolitin IV (ID 3232 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: