Inhibition of L-Alanine Adding Enzyme by Glycine
نویسندگان
چکیده
منابع مشابه
Absorption of glycine and L-alanine by the human jejunum.
Most, if not all, ingested protein is degraded into amino acids, which are then absorbed. Absorption of amino acids has been studied in intact animals, everted gut sacs, and in other preparations of intestine. These studies have been reviewed recently (1, 2). Comparatively little is known, however, about amino acid absorption in the human. Kuroda and Gimbel (3) showed that when racemic amino ac...
متن کاملTemperature-sensitive mutants of Escherichia coli K-12 with low activities of the L-alanine adding enzyme and the D-alanyl-D-alanine adding enzyme.
A number of properties of temperature-sensitive mutants in murein synthesis are described. The mutants grow at 30 C but lyse at 42 C. One mutant possesses a temperature-sensitive d-alanyl-d-alanine adding enzyme, has an impaired rate of murein synthesis in vivo at both 30 and 42 C, and contains elevated levels of uridine diphosphate-N-acetyl-muramyl-tripeptide (UDP-MurNAc-l-Ala-d-Glu-m-diaminop...
متن کاملAffinity labeling of alanine aminotransferase by 3-chloro-L-alanine.
The pyridoxal form of alanine aminotransferase from pig heart catalyzes the a,/? elimination reaction with 3chloro-L-alanine as the substrate to form equimolar amounts of pyruvate, ammonia, and chloride. The maximum rate of the a,/3 elimination reaction was 2.5 pmol/min/mg at pH 7.0 (25”(Z), approximately 0.5% that of the transamination reaction between L-alanine and 2-oxoglutarate. Time-depend...
متن کاملGlycine-alanine repeats impair proper substrate unfolding by the proteasome.
Proteasome ATPases unravel folded proteins. Introducing a sequence containing only glycine and alanine residues (GAr) into substrates can impair their digestion. We previously proposed that a GAr interferes with the unfolding capacity of the proteasome, leading to partial degradation of products. Here we tested that idea in several ways. Stabilizing or destabilizing a folded domain within subst...
متن کاملAdding L-3-(2-Naphthyl)alanine to the genetic code of E. coli.
An unnatural amino acid, L-3-(2-naphthyl)alanine, has been site-specifically incorporated into proteins in Escherichia coli. An orthogonal aminoacyl-tRNA synthetase was evolved that uniquely aminoacylates the unnatural amino acid onto an orthogonal amber suppressor tRNA, which delivers the acylated amino acid in response to an amber nonsense codon with translational fidelity greater than 99%. T...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1971
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.35.2050