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Article

Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis.

Chemistry & biology - 25 Aug 2008

Zvonok Nikolai, Pandarinathan Lakshmipathi, Williams John, Johnston Meghan, Karageorgos Ioannis, Janero David R, Krishnan Srinivasan C, Makriyannis Alexandros

Abstract excerpt

The active site of recombinant hexa-histidine-tagged human monoacylglycerol lipase (hMGL) is characterized by mass spectrometry using the inhibitors 5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide (AM6701), and N-arachidonylmaleimide (NAM) as probes. Carbamylation of Ser(129) by AM6701 in the putative hMGL catalytic triad demonstrates this residue's essential role in catalysis. Partial NAM...

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Identifiers

PMID: 18721756
DOI: 10.1016/j.chembiol.2008.06.008
PMCID: PMC3972761

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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