Rat liver polysome N alpha-acetyltransferase: substrate specificity.

  title={Rat liver polysome N alpha-acetyltransferase: substrate specificity.},
  author={Rika Yamada and Ralph A Bradshaw},
  volume={30 4},
The substrate specificity of polysome rat liver N alpha-acetyltransferase (NAT) has been examined by utilizing a series of synthetic and natural substrates that has been systematically altered with respect to N-terminal sequence and length. Families of peptides of the structure S-Y-S-G-G-L-L-L were generated by successively replacing the N-terminal serine, the penultimate tyrosine, and the antepenultimate serine with all 19 commonly occurring amino acids, which were then assessed for their… 
Specificity determinants of acylaminoacyl‐peptide hydrolase
  • R. Krishna, F. Wold
  • Biology, Chemistry
    Protein science : a publication of the Protein Society
  • 1992
It appears that there is a general effect of the overall sequence of each peptide, and that the specific effects of individual residues are modulated significantly by the environment (context) in which they are expressed.
Amino-terminal processing of actins mutagenized at the Cys-1 residue.
Studies on the specificity of acetylaminoacylpeptide hydrolase
Compared as substrates for the enzyme acetylaminoacyl‐peptide hydrolase, a number of short (2‐5 residues) acetylated peptides have been compared and it is clear that the properties of the individual substrates reflect the total make‐up of each peptide and not only the effect of a single residue in a given position.
Predicting N-terminal acetylation based on feature selection method.
  • Yu-Dong Cai, Lin Lu
  • Biology, Computer Science
    Biochemical and biophysical research communications
  • 2008
Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*
The amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation andN-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues.
N-Terminal Acetylation of Mutationally Altered Form of Iso-1-Cytochromes c in Normal and nat1 - Strains Deficient in the Major N-Terminal Acetyl Transferase of the Yeast Saccharomyces Cerevisiae
The two co-translational processes, cleavage of N-terminal methionine and N-terminal acylation, are by far the most common modification events, affecting nearly all proteins. Protein synthesis
Identification and specificities of N‐terminal acetyltransferases from Saccharomyces cerevisiae
The three N‐terminal acetyltransferases, Ard1p/Nat1p, Nat3p and Mak3p, are significantly related to each other by amino acid sequence, as is Nat3P, which was uncovered in this study using programming alignment procedures.
Membrane topology of liver microsomal cytochrome P450 2B4 determined via monoclonal antibodies directed to the halt-transfer signal.
The membrane topology of cytochrome P450 2B4 from the endoplasmic reticulum has been studied with highly-purified liver microsomes in a site-directed immunochemical approach and ELISA assays showed that all of the antibodies exhibited strong binding to intact microsome.


Specificity of cotranslational amino-terminal processing of proteins in yeast.
The results define the specificity of these enzymes in situ and suggest that the nature of the penultimate amino-terminal residue is the major determinant of their selectivity.
Structures of N-terminally acetylated proteins.
The results suggest that alpha-amino-acetylated proteins have special residues in N-terminally non-hydrophobic structures, compatible with a protective function for acetylation but do not exclude further role(s) in processing or other special functions.
The mechanism of N-terminal acetylation of proteins.
N alpha-acetylation is almost exclusively restricted to eukaryotic structural proteins and appears to have a narrow substrate specificity, which is very similar for enzymes from different tissues and species.
Purification and characterization of hen oviduct N alpha-acetyltransferase.
It is suggested that a thiol group(s) is essential to the enzyme activity of N alpha-acetyltransferase, which recognizes a minute difference in the side chain structure at the N termini of ACTH1-18-NH2 and [Gly1]ACTH1- 18- NH2, a productive and a nonproductive substrate, respectively.
Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
From the results, methionine excision catalyzed by MAP is shown to obey the following rule: the catalytic efficiency of MAP, and therefore the extent of cleavage, decreases in parallel with the increasing of the maximal side-chain length of the amino acid in the penultimate position.
Hen oviduct N alpha-acetyltransferase is a ribonucleoprotein having 7 S RNA.
N alpha-Acetyltransferase lost its activity partially or completely by digestion with bovine pancreatic RNase A, Staphylococcus aureus nuclease, or proteinase K, showing that both the nucleic acid and the protein subunit were necessary for the enzyme activity.
Methionine or not methionine at the beginning of a protein
Methionine aminopeptidases with a universal specificity have been revealed from the sequences of the amino‐terminal region of mutant forms of yeast iso‐1‐cytochrome c and from a systematic