BIOPEP-UWM: Report

ID 2792
Name Precursor of polyphemusin II from homocytes of horse shoe crab
sequence
RRWCFRVCYKGFCYRKCRG
Function:
Precursor of antibacterial peptide
 
Number of residues
19
Activity code
ab
Activity :
antibacterial
Chemical mass 2487.9954 Monoisotopic mass 2486.1935
EC50 :
0.00 µM


Bibliographic data:
Authors
Miyata T, Tokunaga F, Yonega T, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y.
Title
Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. J. Biochem., 106, 663-668, 1989
Year Source
1989 Journal


Additional information:
BIOPEP-UWM database of bioactive peptides

SMILES:
[H][C@](N)(CCCNC(N)=N)C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N[C@@]([H])(Cc1c[nH]c2ccccc12)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCCCN)C(=O)NCC(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)NCC(O)=O

InChI=1S/C110H167N37O22S4/c1-60(2)88(147-95(159)76(32-19-47-128-110(122)123)138-98(162)78(49-62-22-7-4-8-23-62)139-103(167)84(58-172)145-100(164)81(52-65-53-129-70-26-10-9-24-68(65)70)142-93(157)74(30-17-45-126-108(118)119)133-89(153)69(113)25-15-43-124-106(114)115)105(169)146-85(59-173)104(168)141-79(50-63-33-37-66(148)38-34-63)97(161)134-71(27-11-13-41-111)90(154)130-54-86(150)132-77(48-61-20-5-3-6-21-61)96(160)144-83(57-171)102(166)140-80(51-64-35-39-67(149)40-36-64)99(163)137-75(31-18-46-127-109(120)121)92(156)136-73(28-12-14-42-112)94(158)143-82(56-170)101(165)135-72(29-16-44-125-107(116)117)91(155)131-55-87(151)152/h3-10,20-24,26,33-40,53,60,69,71-85,88,129,148-149,170-173H,11-19,25,27-32,41-52,54-59,111-113H2,1-2H3,(H,130,154)(H,131,155)(H,132,150)(H,133,153)(H,134,161)(H,135,165)(H,136,156)(H,137,163)(H,138,162)(H,139,167)(H,140,166)(H,141,168)(H,142,157)(H,143,158)(H,144,160)(H,145,164)(H,146,169)(H,147,159)(H,151,152)(H4,114,115,124)(H4,116,117,125)(H4,118,119,126)(H4,120,121,127)(H4,122,123,128)/t69-,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,88-/m0/s1

InChIKey=FMKIMEWLCVSUNZ-XJWXWJRCSA-N


Gly was added at C-terminus, because the active form of this peptide is C-terminal amide. This peptide is active against G(+) and G(-) bacteria. BBA 1197,109-131(1994).

Peptide is the precursor of polyphemusin II (ID 2793 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: