BIOPEP-UWM: Report

ID 2593
Name Precursor of tenecin-1 (1-15)
sequence
VTCDILSVEAKGVKLG
Function:
Precursor of antimicrobial peptide
 
Number of residues
16
Activity code
ab
Activity :
antibacterial
Chemical mass 1631.9280 Monoisotopic mass 1630.8934
EC50 :
0.00 µM


Bibliographic data:
Authors
Lee K. H., Hong Y. S., Oh J. E., Kwon M., Yoon J. H., Lee J., Lee B. L., Moon H. M.
Title
Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor. Biochem. J., 334, 99-105 (1998).
Year Source
1998 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(N[C@](C(N[C@](C(NCC(N[C@](C(N[C@](C(N[C@](C(NCC(O)=O)=O)(CC(C)C)[H])=O)(CCCCN)[H])=O)(C(C)C)[H])=O)=O)(CCCCN)[H])=O)(C)[H])=O)(CCC(O)=O)[H])=O)(C(C)C)[H])=O)(CO)[H])=O)(CC(C)C)[H])=O)([C@@H](C)CC)[H])=O)(CC(O)=O)[H])=O)(CS)[H])=O)([C@@H](C)O)[H])=O)(C(C)C)[H]

InChI=1S/C71H126N18O23S/c1-15-38(12)56(88-64(105)46(28-51(95)96)82-66(107)48(32-113)85-71(112)57(40(14)91)89-67(108)53(74)35(6)7)70(111)83-45(27-34(4)5)63(104)84-47(31-90)65(106)87-55(37(10)11)69(110)80-43(22-23-50(93)94)61(102)77-39(13)58(99)78-41(20-16-18-24-72)59(100)75-29-49(92)86-54(36(8)9)68(109)79-42(21-17-19-25-73)62(103)81-44(26-33(2)3)60(101)76-30-52(97)98/h33-48,53-57,90-91,113H,15-32,72-74H2,1-14H3,(H,75,100)(H,76,101)(H,77,102)(H,78,99)(H,79,109)(H,80,110)(H,81,103)(H,82,107)(H,83,111)(H,84,104)(H,85,112)(H,86,92)(H,87,106)(H,88,105)(H,89,108)(H,93,94)(H,95,96)(H,97,98)/t38-,39-,40+,41-,42-,43-,44-,45-,46-,47-,48-,53-,54-,55-,56-,57-/m0/s1

InChIKey: RRGUAPNCQQPSTG-FVPCKDGLSA-N


This fragment shows activity against fungi and G(+) bacteria. The active form of this fragment is C-terminal amide, so Gly was added.

Peptide is the precursor of antibacterial peptide (ID 2594 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: