N.m.r. studies of enzyme mechanism. Comparison of the crystal structure and solid state 13C and 15N n.m.r. spectra of a carboxypeptidase A complex with glycyl tyrosine
- 1 January 1985
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Chemical Communications
- No. 10,p. 635-637
- https://doi.org/10.1039/c39850000635
Abstract
It is shown that solid state n.m.r. spectroscopy can be used to determine the extent of cleavage of the scissile amide bond in glycyl tyrosine, a slow substrate for the enzyme carboxypeptidase A in the crystalline enzyme substrate complex.Keywords
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