BIOPEP-UWM: Report

ID 3230
Name Bombolitin V precursor
sequence
INVLGILGLLGKALSHLG
Function:
Precursor of hemolytic peptide
 
Number of residues
18
Activity code
he
Activity :
haemolytic
Chemical mass 1788.1763 Monoisotopic mass 1787.0999
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: [C@@H](C)(NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)[C@@H](C)CC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CN=C[N]1)C(=O)N[C@@H](CC(C)C)C(=O)NCC(O)=O

InChI=1S/C83H146N22O21/c1-20-48(17)67(86)81(124)100-60(33-62(85)107)79(122)105-68(47(15)16)82(125)101-55(28-43(7)8)72(115)90-37-65(110)104-69(49(18)21-2)83(126)102-56(29-44(9)10)73(116)89-36-64(109)95-57(30-45(11)12)76(119)97-53(26-41(3)4)71(114)88-35-63(108)94-52(24-22-23-25-84)75(118)93-50(19)70(113)96-58(31-46(13)14)77(120)103-61(39-106)80(123)99-59(32-51-34-87-40-92-51)78(121)98-54(27-42(5)6)74(117)91-38-66(111)112/h34,40-50,52-61,67-69,106H,20-33,35-39,84,86H2,1-19H3,(H2,85,107)(H,87,92)(H,88,114)(H,89,116)(H,90,115)(H,91,117)(H,93,118)(H,94,108)(H,95,109)(H,96,113)(H,97,119)(H,98,121)(H,99,123)(H,100,124)(H,101,125)(H,102,126)(H,103,120)(H,104,110)(H,105,122)(H,111,112)/t48-,49-,50-,52-,53-,54-,55-,56-,57-,58-,59-,60-,61-,67-,68-,69-/m0/s1

InChIKey=BFRYSDAMZKMCAL-SHIOJCJBSA-N


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

Peptide is the precursor of Bombolitin V (ID 3231 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: