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Issue 8, 2012
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l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

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Abstract

Serine palmitoyltransferase (SPT) catalyses the first committed step of de novo sphingolipid biosynthesis. The bacterial SPT homologue from Sphingomonas paucimobilis is a homodimeric enzyme that contains an essential pyridoxal-5′-phosphate (PLP) cofactor bound to each subunit. Inhibitors of SPT are useful blockers of sphingolipid biosynthesis. Here we use UV-vis spectroscopy, enzyme kinetics and mass spectrometry to investigate inhibition of SPT by penicillamine (Pen), a drug with a range of useful medicinal applications.

Graphical abstract: l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

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Publication details

The article was received on 27 Jan 2012, accepted on 05 Apr 2012 and first published on 17 Apr 2012


Article type: Concise Article
DOI: 10.1039/C2MD20020A
Med. Chem. Commun., 2012,3, 1003-1008

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    L-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

    J. Lowther, A. E. Beattie, P. R. R. Langridge-Smith, D. J. Clarke and D. J. Campopiano, Med. Chem. Commun., 2012, 3, 1003
    DOI: 10.1039/C2MD20020A

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