Asatoor

Bagdanoff

Beesley

Bourquin

Buell

Evered

Hanada

Heyl

Kuchinskas

Lowther

Mackay

Matsuo

O'Leary

Raman

Saba

Saiz

Schonbeck

Sukanya

Tanase

Terzuoli

Walshe

Weigert

Wilson

Woodward

Yanagidani

Yard

Jonathan Lowther

Ashley E. Beattie

Pat R. R. Langridge-Smith

David J. Clarke

Dominic J. Campopiano

Crossref

MedChemComm

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

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.</p

Lowther, Jonathan

Beattie, Ashley E.

Langridge-Smith, Pat R. R.

Clarke, David J.

Campopiano, Dominic J.

Edinburgh Research Explorer

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

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

Abstract

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Edinburgh Research Explorer