NDLI: The Modification of the Peptidyltransferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Pyridoxal Phosphate

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The Modification of the Peptidyltransferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Pyridoxal Phosphate

Content Provider	Scilit
Author	Baxter, Ross M. White, Vivienne T. Zahid, Nasir D.
Copyright Year	1980
Description	Journal: Journal of Biological Inorganic Chemistry Pyridoxal phosphate photoinactivates the peptidyltransferase activity of 50-S ribosomal subunits, LiCl split proteins and protein L16. Ethyromycin exhibits significant protection. These results, taken together with earlier reports, indicate the involvement of the single histidine of L16 in peptidyltransferase activity. The adjacent association in L16 of histidine and lysine indicates that pyridoxal phosphate should represent a selective inhibitor of peptidyltransferase activity.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1980.tb04851.x/pdf
Ending Page	166
Page Count	6
Starting Page	161
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1980.tb04851.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	1
Volume Number	110
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1980-09-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Peptidyltransferase Activity Pyridoxal Phosphate
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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