BIOPEP-UWM: Report

ID 3233
Name Precursor of Bombolitin IV
sequence
INIKDILAKLVKVLGHVG
Function:
Precursor of hemolytic peptide
 
Number of residues
18
Activity code
he
Activity :
haemolytic
Chemical mass 1930.3746 Monoisotopic mass 1929.2102
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])(CCCCN)NC(=O)[C@@]([H])(NC(=O)[C@]([H])(CC(N)=O)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)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N[C@@]([H])(CC1=CN=CN1)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(O)=O

InChI=1S/C90H160N24O22/c1-20-51(16)69(95)85(131)107-63(39-65(94)115)83(129)113-73(52(17)21-2)89(135)104-57(30-24-27-33-92)78(124)106-64(40-67(117)118)84(130)114-74(53(18)22-3)90(136)109-60(36-46(6)7)80(126)100-54(19)75(121)102-56(29-23-26-32-91)77(123)105-61(37-47(8)9)81(127)112-71(49(12)13)87(133)103-58(31-25-28-34-93)79(125)111-72(50(14)15)88(134)108-59(35-45(4)5)76(122)97-42-66(116)101-62(38-55-41-96-44-99-55)82(128)110-70(48(10)11)86(132)98-43-68(119)120/h41,44-54,56-64,69-74H,20-40,42-43,91-93,95H2,1-19H3,(H2,94,115)(H,96,99)(H,97,122)(H,98,132)(H,100,126)(H,101,116)(H,102,121)(H,103,133)(H,104,135)(H,105,123)(H,106,124)(H,107,131)(H,108,134)(H,109,136)(H,110,128)(H,111,125)(H,112,127)(H,113,129)(H,114,130)(H,117,118)(H,119,120)/t51-,52-,53-,54-,56-,57-,58-,59-,60-,61-,62-,63-,64-,69-,70-,71-,72-,73-,74-/m0/s1

InChIKey=IUUGAISUPANVER-FUTXVYEKSA-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: