= W. K. Yip
{c}
<W. K. Yip> is the first author of a 1990 study probing the <active site> of <1-aminocyclopropane-1-carboxylate synthase>, an <enzyme> involved in <Ethylene> production in <plants>. The <enzyme> uses <pyridoxal phosphate> and acts on <S-adenosylmethionine>, but its own <substrate> can also inactivate it. The study investigated the chemistry underlying that apparent paradox.<Characterization and sequencing of the active site of 1-aminocyclopropane-1-carboxylate synthase by W. K. Yip and others>[Abstract; PNAS 87, 7930–7934, 1990]{ref}
The researchers labeled purified apple <enzyme>, cut it into <peptides> and separated the products by <high-performance liquid chromatography>. <Peptide sequencing> and <mass spectrometry> located a modified <lysine residue> in an <active site> peptide. Their results connected the same <lysine residue> with binding <pyridoxal phosphate> and with covalent attachment of a fragment derived from the <substrate> during inactivation. Rather than merely observing that an <enzyme> stopped working, the experiments identified the modified site and constrained the chemical explanation.<Characterization and sequencing of the active site of 1-aminocyclopropane-1-carboxylate synthase by W. K. Yip and others>[Abstract: radioactive labeling, shared active-site peptide, hydrolysis and mass-spectrometric identification]{ref}
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