Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism.
Rudnick, D A
Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Feb 1993 - 1087-91 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.90.3.1087 doi
Acyl Coenzyme A--metabolism
Acyltransferases--metabolism
Amino Acid Sequence
Azides--metabolism
Binding Sites
Cross-Linking Reagents
Kinetics
Molecular Sequence Data
Oligopeptides--metabolism
Protein Processing, Post-Translational
Saccharomyces cerevisiae--enzymology
Substrate Specificity
Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Feb 1993 - 1087-91 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.90.3.1087 doi
Acyl Coenzyme A--metabolism
Acyltransferases--metabolism
Amino Acid Sequence
Azides--metabolism
Binding Sites
Cross-Linking Reagents
Kinetics
Molecular Sequence Data
Oligopeptides--metabolism
Protein Processing, Post-Translational
Saccharomyces cerevisiae--enzymology
Substrate Specificity