BIOPEP-UWM: Report

ID 2596
Name Precursor of tachylepsin III from homocytes of horse shoe crab
sequence
KWCFRVCYRGICYRRCRG

Function:
Precursor of antimicrobial peptide
 
Number of residues
18
Activity code
ab
Activity :
antibacterial
Chemical mass 2325.8073 Monoisotopic mass 2324.1144
EC50 :
0.00 µM



Bibliographic data:
Authors
Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S.
Title
Tachyplesin, a class of antimocrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem., 263, 16709-16713, 1988
Year Source
1988 Journal



Additional information:
BIOPEP-UWM database of bioactive peptides

SMILES: [H][C@](N)(CCCCN)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])(CCCNC(N)=N)C(=O)NCC(=O)N[C@]([H])(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])(CCCNC(N)=N)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)NCC(O)=O)[C@@]([H])(C)CC


InChI=1S/C101H157N35O21S4/c1-5-54(4)80(96(157)134-76(52-161)94(155)130-71(44-57-30-34-60(138)35-31-57)89(150)125-66(25-15-39-116-99(108)109)84(145)124-67(26-16-40-117-100(110)111)85(146)131-73(49-158)91(152)123-65(24-14-38-115-98(106)107)83(144)121-48-78(140)141)135-77(139)47-120-82(143)64(23-13-37-114-97(104)105)122-87(148)70(43-56-28-32-59(137)33-29-56)129-93(154)75(51-160)133-95(156)79(53(2)3)136-86(147)68(27-17-41-118-101(112)113)126-88(149)69(42-55-18-7-6-8-19-55)128-92(153)74(50-159)132-90(151)72(127-81(142)62(103)21-11-12-36-102)45-58-46-119-63-22-10-9-20-61(58)63/h6-10,18-20,22,28-35,46,53-54,62,64-76,79-80,119,137-138,158-161H,5,11-17,21,23-27,36-45,47-52,102-103H2,1-4H3,(H,120,143)(H,121,144)(H,122,148)(H,123,152)(H,124,145)(H,125,150)(H,126,149)(H,127,142)(H,128,153)(H,129,154)(H,130,155)(H,131,146)(H,132,151)(H,133,156)(H,134,157)(H,135,139)(H,136,147)(H,140,141)(H4,104,105,114)(H4,106,107,115)(H4,108,109,116)(H4,110,111,117)(H4,112,113,118)/t54-,62-,64-,65-,66-,67-,68-,69-,70-,71-,72-,73-,74-,75-,76-,79-,80-/m0/s1

InChIKey=DDWWEUQOICXGLB-IXZDDLHDSA-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 antibacterial peptide (ID 2595 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: