2. Anti-infection
  3. Bacterial Antibiotic
  4. Kirromycin

Kirromycin  (Synonyms: Mocimycin; Delvomycin)

製品番号: HY-122386
取扱説明書 Technical Support

Kirromycin (Mocimycin; Delvomycin) is an elongation factor Tu (EF-Tu) inhibitor targeting protein biosynthesis. As an antibiotic, Kirromycin exerts antibacterial activity against Gram-negative bacteria by acting on EF-Tu to interfere with the peptidyl transfer reaction. Kirromycin is applicable to studies on bacterial infections.

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Kirromycin

Kirromycin 構造式

CAS 番号 : 50935-71-2

容量 価格（税別） 在庫状況 数量
500 μg $877 お問い合わせ 3 - 4 Weeks 4 - 5 Weeks 5 - 6 Weeks 2 - 3 weeks
1 mg $1700 お問い合わせ 3 - 4 Weeks 4 - 5 Weeks 5 - 6 Weeks 2 - 3 weeks
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Kirromycin 関連抗体

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製品説明

Kirromycin (Mocimycin; Delvomycin) is an elongation factor Tu (EF-Tu) inhibitor targeting protein biosynthesis. As an antibiotic, Kirromycin exerts antibacterial activity against Gram-negative bacteria by acting on EF-Tu to interfere with the peptidyl transfer reaction. Kirromycin is applicable to studies on bacterial infections[1][2][3].

体外実験

Kirromycin (5 min) potently inhibits poly (U)-directed polyphenylalanine synthesis in an *E. coli* cell-free translation system, with an IC50 of 5 × 10-7 M[1].
Kirromycin (5 min) doubles the EF-T-dependent GTP hydrolysis activity, strongly inhibits EF-T-dependent peptide bond formation, and does not alter EF-T-mediated binding of Phe-tRNAPhe to ribosomes in the *Escherichia coli* ribosome assay system[1].
When incubated with EF-T and GTP for 5 min, kirromycin increases the binding amount of [3H]GTP to *Escherichia coli* EF-T to more than three times the original level[1].
Kirromycin (500 pmol; 10 min) induces Escherichia coli EF-T-dependent GTP hydrolysis in the absence of ribosomes or aminoacyl-tRNA; this activity is specifically activated only in the presence of Phe-tRNAPhe (but not uncharged tRNAPhe or Ac-Phe-tRNAPhe); it significantly enhances this activity in the presence of ribosomes; its GTP Km is 2 × 10-7 M, which is consistent with the GTP Km of ribosome- and Phe-tRNAPhe-dependent EF-T GTPase in the absence of antibiotics[1].
Kirromycin (1 nmol; 5 min) enables EF-T-dependent binding of Phe-tRNAPhe to poly (U)-ribosome complexes in *E. coli* in the absence of GTP, with the amount of [14C]Phe-tRNAPhe bound to ribosomes reaching 3.5 pmol[1].
At 4°C, kirromycin reduces the affinity of *E. coli* EF-Tu-GTP for aa-tRNA by approximately 3 orders of magnitude, resulting in a Kd of 2 μM; it also equalizes the affinity of *E. coli* EF-Tu-GDP for aa-tRNA to a Kd of 7 μM at 4°C, thereby eliminating the significant difference in affinity between EF-Tu-GTP and EF-Tu-GDP for aa-tRNA observed in the absence of this antibiotic[3].
Kirromycin (0.4-26 μM) binds to EF-Tu-GDP (as well as EF-Tu-GTP) from *E. coli* at a 1:1 molar ratio to form a complex, induces conformational changes that increase the net negative charge and electrophoretic mobility of EF-Tu, and exhibits an extremely low dissociation rate[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Kirromycin 関連抗体
分子量

796.94

分子式

C43H60N2O12
CAS 番号
SMILES

O=C(NC/C=C/C=C(C)/[C@@H](OC)[C@H]([C@]([C@H]([C@H]1O)O)([H])O[C@@H]1/C=C/C=C/C=C(C)/C(C(C2=O)=C(C=CN2)O)=O)C)[C@H]([C@@](O[C@H](C(C)3C)/C=C/C=C\C)([C@@H]([C@@H]3O)O)O)CC
Structure Classification
Initial Source

Streptomyces collinus Tue 365
輸送条件

Room temperature in continental US; may vary elsewhere.
保管条件

Please store the product under the recommended conditions in the Certificate of Analysis.
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Kirromycin Related Classifications

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Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

Keywords:

Kirromycin50935-71-2Mocimycin DelvomycinBacterialAntibioticElongation factor Tu inhibitorantibioticbacteriaInhibitorinhibitorinhibit

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