Met-AMC
Met-AMC is a fluorescent substrate used to detect the activity of methionine aminopeptidase (MetAP). Hydrolysis of the substrate releases the fluorophore AMC, with detection performed at an excitation wavelength of 360 nm and an emission wavelength of 460 nm. Met-AMC can distinguish the effects of different metal cofactors on the substrate preference of MetAP1: Zn (II)-MetAP1 barely hydrolyzes Met-AMC, while Co (II)-, Mn (II)-, and Ni (II)-MetAP1 can stably cleave this substrate. Met-AMC can be used to establish an intracellular MetAP activity cell-based assay system, which quantifies the intracellular MetAP inhibition level by monitoring the fluorescence signal from substrate hydrolysis in living cells.
For research use only. We do not sell to patients.
- CAS No.: 94367-34-7
- Formula: C15H18N2O3S
- Molecular Weight:306.38
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Storage:
Please store the product under the recommended conditions in the Certificate of Analysis.
Biological Activity
Met-AMC is a fluorescent substrate, and the enzymatic activity of E. coli MetAP can be quantified by detecting the fluorescence of released AMC[1].
Met-AMC can be hydrolyzed by purified cobalt-, manganese-, and nickel-substituted EcMetAP1, among which Co-EcMetAP1 exhibits the highest catalytic efficiency (kcat/Km = 2.64 M-1s-1), whereas zinc-substituted EcMetAP1 shows no detectable activity toward Met-AMC[3].
Met-AMC serves as a fluorescent substrate for recombinant E. coli MetAP in permeabilized BL21 (DE3) cells, with optimal permeability and hydrolytic activity observed within the CaCl2 concentration range of 200 µM to 10 mM[2].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Chemical Information
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CAS No. 94367-34-7
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Molecular Weight 306.38
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Formula C15H18N2O3S
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SMILES
CC(C1=CC=C(NC([C@@H](N)CCSC)=O)C=C1O2)=CC2=O
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Please store the product under the recommended conditions in the Certificate of Analysis.
Purity & Documentation
References
[1]. Huang M, et al. Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis. Journal of medicinal chemistry. 2007 Nov 15;50(23):5735-42. [Content Brief]
[2]. Chai SC, et al. Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase. European journal of medicinal chemistry. 2011 Aug;46(8):3537-40. [Content Brief]
[3]. Li JY, et al. Specificity for inhibitors of metal-substituted methionine aminopeptidase. Biochemical and biophysical research communications. 2003 Jul 18;307(1):172-9. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)