BIOPEP-UWM: Report
ID | 2964 |
Name | Precursor of antibacterial peptide |
sequence |
Function: | |||
Precursor of antibacterial peptide | |||
Number of residues | 27 |
Activity code | ab |
Activity : | antibacterial |
|||
Chemical mass | 2783.2129 | Monoisotopic mass | 2781.5800 | |
EC50 : | 0.00 µM |
Bibliographic data: | |
Authors | |
Rozek T., Waugh R. J., Steinborner S. T., Bowie J. H., Tyler M. J., Wallace J. C. | |
Title | |
The Maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of Maculatin 1.1 and Caerin 1.1. J. Pept. Sci. 4, 111-115, 1998 | |
Year | Source |
1998 | Journal |
Additional information: |
BIOPEP-UWM database of bioactive peptides SMILES: NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)NCC(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)O InChI=1S/C123H216N32O40/c1-22-65(16)97(120(192)143-74(34-39-87(128)160)105(177)133-68(19)101(173)132-55-95(171)172)151-91(164)54-131-104(176)84(56-156)150-119(191)96(64(14)15)153-122(194)98(66(17)23-2)152-90(163)53-130-103(175)71(31-25-28-44-124)136-102(174)69(20)134-112(184)80(48-60(6)7)146-117(189)85(57-157)148-110(182)78(38-43-94(169)170)141-116(188)83(51-63(12)13)147-118(190)86(58-158)149-109(181)77(37-42-93(167)168)140-114(186)81(49-61(8)9)144-107(179)72(32-26-29-45-125)137-108(180)76(36-41-92(165)166)138-106(178)73(33-27-30-46-126)142-121(193)99(67(18)24-3)154-123(195)100(70(21)159)155-111(183)75(35-40-88(129)161)139-115(187)82(50-62(10)11)145-113(185)79(47-59(4)5)135-89(162)52-127/h59-86,96-100,156-159H,22-58,124-127H2,1-21H3,(H2,128,160)(H2,129,161)(H,130,175)(H,131,176)(H,132,173)(H,133,177)(H,134,184)(H,135,162)(H,136,174)(H,137,180)(H,138,178)(H,139,187)(H,140,186)(H,141,188)(H,142,193)(H,143,192)(H,144,179)(H,145,185)(H,146,189)(H,147,190)(H,148,182)(H,149,181)(H,150,191)(H,151,164)(H,152,163)(H,153,194)(H,154,195)(H,155,183)(H,165,166)(H,167,168)(H,169,170)(H,171,172)/t65-,66-,67-,68-,69-,70+,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,96-,97-,98-,99-,100-/m0/s1 InChIKey=BGKFRSGBSASAJH-QTDZWGBRSA-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 2963 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: |