𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Demonstration of multiple forms of bovine brain myristoyl CoA: protein N-myristoyl transferase

✍ Scribed by Martin J. King; Raiendra K. Sharma

Publisher
Springer
Year
1992
Tongue
English
Weight
303 KB
Volume
113
Category
Article
ISSN
0300-8177

No coin nor oath required. For personal study only.

✦ Synopsis

Four distinct N-myristoyl transferase (NMT) activity peaks, designated I, II, III, and IV, were separated from the cytosolic fraction of bovine brain by DEAE-Sepharose column chromatography. Peaks I, II, III and IV were characterised biochemically with respect to substrate specificity: with cAMP-dependent protein kinase and pp60src derived peptides, and by their apparent molecular mass. The apparent molecular mass of peaks I, II, III and IV were 190 kDa, 224 kDa, 390 kDa and 76 kDa, respectively. These results indicate that bovine brain contains multiple forms of NMT.

πŸ“œ SIMILAR VOLUMES

An Assay for Myristoyl-CoA:Protein N-Myr
An Assay for Myristoyl-CoA:Protein N-Myristoyltransferase Activity Based on Ion-Exchange Exclusion of [3H] Myristoyl Peptide
✍ S.A. French; H. Christakis; R.R. Oneill; S.P.F. Miller πŸ“‚ Article πŸ“… 1994 πŸ› Elsevier Science 🌐 English βš– 552 KB

We developed an assay to test for inhibition of myristoyl-CoA:protein \(\mathbf{N}\)-myristoyltransferase (NMT) activity since this enzyme is important in viral replication and cellular biochemistry. Saccharomyces cerevisae NMT was harvested from Escherichia coli carrying a plasmid vector containing

Replacements for lysine in l-seryl-l-lys
Replacements for lysine in l-seryl-l-lysyl dipeptide amide inhibitors of candida albicans myristoyl-CoA:protein N-myristoyltransferase
✍ David L. Brown; Balekudru Devadas; Hwang-Fun Lu; Srinivasan Nagarajan; Mark E. Z πŸ“‚ Article πŸ“… 1997 πŸ› Elsevier Science 🌐 English βš– 225 KB

A survey of potential cyclic and acyclic lysine replacements in known L-seryl-L-lysyl dipeptide inhibitors of C. albicans NMT identified the thioether 16 and glycinamide 18 as submicromolar inhibitors of C. albicans NMT, which retained good selectivity over the human enzyme. All of the heterocyclic