94367-34-7
Chemical Structure
Met-AMC
- CAS No.: 94367-34-7
- Formula:C15H18N2O3S
- Molecular Weight:306.38
InChIKey: FHLNBHBQGFIHKH-LBPRGKRZSA-N
SMILES: CC(C1=CC=C(NC([C@@H](N)CCSC)=O)C=C1O2)=CC2=O
Biological Activity: 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[1][2][3].
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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. | |||||||||||||||||||||
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- [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]
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