Issue 10, 1985

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

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.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1985, 635-637

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

N. E. Mackenzie, P. E. Fagerness and A. I. Scott, J. Chem. Soc., Chem. Commun., 1985, 635 DOI: 10.1039/C39850000635

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