BIOPEP-UWM: Report

ID 2592
Name Precursor of tenecin-1 (16-32)
sequence
NDAACAAHCLFRGRSGGG
Function:
Precursor of antimicrobial peptide
 
Number of residues
18
Activity code
ab
Activity :
antibacterial
Chemical mass 1762.9252 Monoisotopic mass 1761.7764
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(N[C@](C(NCC(N[C@](C(N[C@](C(NCC(NCC(NCC(O)=O)=O)=O)=O)(CO)[H])=O)(CCCNC(N)=N)[H])=O)=O)(CCCNC(N)=N)[H])=O)(Cc1ccccc1)[H])=O)(CC(C)C)[H])=O)(CS)[H])=O)(Cc1[nH]cnc1)[H])=O)(C)[H])=O)(C)[H])=O)(CS)[H])=O)(C)[H])=O)(C)[H])=O)(CC(O)=O)[H])=O)(CC(N)=O)[H]

InChI=1S/C70H111N27O23S2/c1-32(2)18-42(64(116)94-43(19-37-12-8-7-9-13-37)65(117)90-40(14-10-16-78-69(73)74)60(112)83-26-52(102)89-41(15-11-17-79-70(75)76)62(114)95-46(28-98)61(113)82-25-51(101)80-24-50(100)81-27-54(105)106)93-68(120)48(30-122)97-66(118)44(20-38-23-77-31-84-38)91-57(109)35(5)85-56(108)34(4)88-67(119)47(29-121)96-58(110)36(6)86-55(107)33(3)87-63(115)45(22-53(103)104)92-59(111)39(71)21-49(72)99/h7-9,12-13,23,31-36,39-48,98,121-122H,10-11,14-22,24-30,71H2,1-6H3,(H2,72,99)(H,77,84)(H,80,101)(H,81,100)(H,82,113)(H,83,112)(H,85,108)(H,86,107)(H,87,115)(H,88,119)(H,89,102)(H,90,117)(H,91,109)(H,92,111)(H,93,120)(H,94,116)(H,95,114)(H,96,110)(H,97,118)(H,103,104)(H,105,106)(H4,73,74,78)(H4,75,76,79)/t33-,34-,35-,36-,39-,40-,41-,42-,43-,44-,45-,46-,47-,48-/m0/s1

InChIKey: CXYSVXMNFCHZRM-AMRFPLJWSA-N


The active form of this peptide contains C-terminal amide group instead of C-terminal glycine residue.

Peptide is the precursor of antibacterial peptide (ID 2591 in BIOPEP 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: