N.M.R. studies of enzyme mechanism: Comparison of the crystal structure and solid state super(13)C and super(15)N N.M.R. spectra of a carboxypeptidase A complex with glycyl tyrosine

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.

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Bibliographic Details
Published in:Journal of the Chemical Society. Chemical communications 1985-01 (10), p.635-636
Main Authors: Mackenzie, N E, Fagerness, P E, Scott, AI
Format: Article
Language:English
Subjects:
carboxypeptidase A
glycyl-L-tyrosine
N.M.R
Online Access:Get full text
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Description
Summary: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.
ISSN:0022-4936