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Merck

G1424

Sigma-Aldrich

Globomycin from Streptomyces hagronensis

Synonym(e):

Globomycin, Glycine, N-(N-(N-(N-(N-(3-hydroxy-2-methyl-1-oxononyl)-N-methylleucyl)-L-alloisoleucyl)-L-seryl)-L-allothreonyl)-, rho-lactone, SF 1902

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About This Item

Empirische Formel (Hill-System):
C32H57N5O9
CAS-Nummer:
Molekulargewicht:
655.82
MDL-Nummer:
UNSPSC-Code:
51102829
NACRES:
NA.85

Biologische Quelle

Streptomyces hagronensis

Qualitätsniveau

Assay

≥98% (HPLC)

Form

powder

Farbe

white

Löslichkeit

DMSO: 1 mg/mL

Wirkungsspektrum von Antibiotika

Gram-negative bacteria

Wirkungsweise

enzyme | inhibits

Lagertemp.

−20°C
−20°C

InChI

1S/C32H57N5O9/c1-9-11-12-13-14-24-20(6)32(45)37(8)23(15-18(3)4)29(42)35-26(19(5)10-2)31(44)34-22(17-38)28(41)36-27(21(7)39)30(43)33-16-25(40)46-24/h18-24,26-27,38-39H,9-17H2,1-8H3,(H,33,43)(H,34,44)(H,35,42)(H,36,41)

InChIKey

VFGBXFZXJAWPOE-UHFFFAOYSA-N

Allgemeine Beschreibung

Globomycin is a cyclic peptide antibiotic, which inhibits the growth of enteric Gram-negative bacteria through cell wall synthesis inhibition.

Anwendung


  • Globomycin, a new peptide antibiotic with spheroplast-forming activity. I. Taxonomy of producing organisms and fermentation.: This study explores the taxonomy of the producing organisms of Globomycin and details the fermentation processes involved. This antibiotic shows spheroplast-forming activity, indicating its potential application in targeting bacterial cell wall synthesis (Inukai et al., 1978).

Biochem./physiol. Wirkung

Globomycin was found to inhibit LspA, a lipoprotein signal peptidase. It eliminates the maturation of pro-lipoproteins by inhibition of the enzyme that converts pro-lipoprotein to lipoprotein, acting as a substrate analog of the signal sequence in the outer membrane of Gram-negative bacteria.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

D A Haake et al.
Infection and immunity, 66(4), 1579-1587 (1998-04-07)
We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment in order to design an oligonucleotide probe. A Lambda-Zap II library
Mikio Shoji et al.
Molecular microbiology, 52(5), 1513-1525 (2004-05-29)
Bacterial cell surface filaments play significant roles in adherence to and invasion of host cells. They are generated by the chaperone/usher pathway system (class I fimbriae), the type II secretion system (type IV pili) and the nucleation-dependent polymerization system (Curli
Henry S Gibbons et al.
Journal of bacteriology, 189(14), 5090-5100 (2007-05-15)
The SecA2 protein is part of a specialized protein export system of mycobacteria. We set out to identify proteins exported to the bacterial cell envelope by the mycobacterial SecA2 system. By comparing the protein profiles of cell wall and membrane
Toshihiro Kiho et al.
Drug design and discovery, 18(4), 109-116 (2004-11-24)
Globomycin (1), a 19-membered cyclic depsipeptide, exhibited an antibiotic activity against gram-negative bacteria by inhibiting signal peptidase II in the cytoplasmic membrane. Although only one conformation of 1 was observed for the crystal structure, it was revealed by 1H NMR
H Loferer et al.
Molecular microbiology, 26(1), 11-23 (1998-01-31)
Curli, an adhesive surface fibre produced by Escherichia coli and salmonellae, was proposed on the basis of genetic evidence to follow a distinct assembly pathway involving an extracellular intermediate of the fibre subunit CsgA, the polymerization of which can be

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