BIOPEP-UWM: Report

ID 7857
Name Neuropeptide precursor
sequence
GLFDVIKKVASVIGGLG

Function:
Neuropeptide precursor
 
Number of residues
17
Activity code
inh
Activity :
inhibitor
Chemical mass 1673.0000 Monoisotopic mass 1671.9892
EC50 :
0.00 µM



Bibliographic data:
Authors
Doyle J., Llewellyn L. E., Brinkworth C. S., Bowie J. H., Wegener K. L., Rozek T., Wabnitz P. A., Wallace J. C., Tyler M. J.
Title
Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation of lesuerin from the skin secretion of the Australian Stony Creek frog Litoria lesueuri. Eur. J. Biochem., 269, 100-109, 2002
Year Source
2002 Journal



Additional information:
BIOPEP-UWM database of bioactive peptides


SMILES: NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)NCC(=O)NCC(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)O

InChI=1S/C78H133N19O21/c1-16-45(13)64(74(114)83-36-57(100)82-37-58(101)87-51(31-40(3)4)67(107)84-38-60(104)105)96-76(116)63(44(11)12)95-73(113)55(39-98)92-66(106)47(15)85-75(115)61(42(7)8)93-69(109)50(28-22-24-30-80)88-68(108)49(27-21-23-29-79)89-78(118)65(46(14)17-2)97-77(117)62(43(9)10)94-72(112)54(34-59(102)103)91-71(111)53(33-48-25-19-18-20-26-48)90-70(110)52(32-41(5)6)86-56(99)35-81/h18-20,25-26,40-47,49-55,61-65,98H,16-17,21-24,27-39,79-81H2,1-15H3,(H,82,100)(H,83,114)(H,84,107)(H,85,115)(H,86,99)(H,87,101)(H,88,108)(H,89,118)(H,90,110)(H,91,111)(H,92,106)(H,93,109)(H,94,112)(H,95,113)(H,96,116)(H,97,117)(H,102,103)(H,104,105)/t45-,46-,47-,49-,50-,51-,52-,53-,54-,55-,61-,62-,63-,64-,65-/m0/s1

InChIKey: GSVIUYBLXKWEGD-GCQBAMSOSA-N


The active form is C-terminal amide group instead of C-terminal glycine residue.

Peptide is the precursor of neuropeptide (ID 2889 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: