BIOPEP-UWM: Report

ID 2597
Name Precursor of tachylepsin II from homocytes of horse shoe crab
sequence
RWCFRVCYRGICYRRCRG
Function:
Precursor of antibacterial peptide
 
Number of residues
18
Activity code
ab
Activity :
antibacterial
Chemical mass 2353.8207 Monoisotopic mass 2352.1206
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:
N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(NCC(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(N[C@](C(NCC(O)=O)=O)(CCCNC(N)=N)[H])=O)(CS)[H])=O)(CCCNC(N)=N)[H])=O)(CCCNC(N)=N)[H])=O)(Cc1ccc(O)cc1)[H])=O)(CS)[H])=O)([C@@H](C)CC)[H])=O)=O)(CCCNC(N)=N)[H])=O)(Cc1ccc(O)cc1)[H])=O)(CS)[H])=O)(C(C)C)[H])=O)(CCCNC(N)=N)[H])=O)(Cc1ccccc1)[H])=O)(CS)[H])=O)(Cc1c2ccccc2[nH]c1)[H])=O)(CCCNC(N)=N)[H]

InChI=1S/C101H157N37O21S4/c1-5-53(4)79(95(159)136-75(51-163)93(157)132-70(43-56-29-33-59(140)34-30-56)88(152)127-65(24-14-38-118-99(109)110)83(147)126-66(25-15-39-119-100(111)112)84(148)133-72(48-160)90(154)125-64(23-13-37-117-98(107)108)82(146)123-47-77(142)143)137-76(141)46-122-81(145)63(22-12-36-116-97(105)106)124-86(150)69(42-55-27-31-58(139)32-28-55)131-92(156)74(50-162)135-94(158)78(52(2)3)138-85(149)67(26-16-40-120-101(113)114)128-87(151)68(41-54-17-7-6-8-18-54)130-91(155)73(49-161)134-89(153)71(44-57-45-121-62-21-10-9-19-60(57)62)129-80(144)61(102)20-11-35-115-96(103)104/h6-10,17-19,21,27-34,45,52-53,61,63-75,78-79,121,139-140,160-163H,5,11-16,20,22-26,35-44,46-51,102H2,1-4H3,(H,122,145)(H,123,146)(H,124,150)(H,125,154)(H,126,147)(H,127,152)(H,128,151)(H,129,144)(H,130,155)(H,131,156)(H,132,157)(H,133,148)(H,134,153)(H,135,158)(H,136,159)(H,137,141)(H,138,149)(H,142,143)(H4,103,104,115)(H4,105,106,116)(H4,107,108,117)(H4,109,110,118)(H4,111,112,119)(H4,113,114,120)/t53-,61-,63-,64-,65-,66-,67-,68-,69-,70-,71-,72-,73-,74-,75-,78-,79-/m0/s1

InChIKey: MHMKCXBWKKXPFN-BMSUNONBSA-N


Gly was added at C-terminus, because the active form of this peptide is C-terminal amide.

Peptide is the precursor of antibacterial peptide (ID 2598 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: