scholarly journals Chemical Synthesis ofO-Ethyl-L-homoserine, a New Amino Acid Produced byCorynebacterium Ethanolaminophilum

1968 ◽  
Vol 41 (3) ◽  
pp. 633-635 ◽  
Author(s):  
Yoshikatsu Murooka ◽  
Tokuya Harada ◽  
Yoshiharu Izumi
2020 ◽  
Vol 56 (25) ◽  
pp. 3641-3644
Author(s):  
Shana Wagner ◽  
Babu Sudhamalla ◽  
Philip Mannes ◽  
Sushma Sappa ◽  
Sam Kavoosi ◽  
...  

An improved chemical synthesis, site-specific incorporation and enhanced photo-crosslinking ability of tmdF have been demonstrated in the context of protein–protein interactions.


2019 ◽  
Vol 58 (36) ◽  
pp. 12599-12603 ◽  
Author(s):  
Simon Baldauf ◽  
Dominik Schauenburg ◽  
Jeffrey W. Bode

2019 ◽  
Vol 55 (35) ◽  
pp. 5095-5098 ◽  
Author(s):  
Kui Zhang ◽  
Ismail A. Ahmed ◽  
Huong T. Kratochvil ◽  
William F. DeGrado ◽  
Feng Gai ◽  
...  

Facile chemical synthesis of l-4CN-Trp and incorporation into a pHLIP peptide enabled FRET study on peptide–membrane interactions.


1991 ◽  
Vol 180 (2) ◽  
pp. 1010-1018 ◽  
Author(s):  
H. de Rocquigny ◽  
D. Ficheux ◽  
C. Gabus ◽  
M.-C. Fournié-Zaluski ◽  
J.-L. Darlix ◽  
...  

Microbiology ◽  
2020 ◽  
Vol 166 (12) ◽  
pp. 1129-1135 ◽  
Author(s):  
Bill Söderström ◽  
Alessandro Ruda ◽  
Göran Widmalm ◽  
Daniel O. Daley

Fluorescent d-amino acids (FDAAs) are molecular probes that are widely used for labelling the peptidoglycan layer of bacteria. When added to growing cells they are incorporated into the stem peptide by a transpeptidase reaction, allowing the timing and localization of peptidoglycan synthesis to be determined by fluorescence microscopy. Herein we describe the chemical synthesis of an OregonGreen488-labelled FDAA (OGDA). We also demonstrate that OGDA can be efficiently incorporated into the PG of Gram-positive and some Gram-negative bacteria, and imaged by super-resolution stimulated emission depletion (STED) nanoscopy at a resolution well below 100 nm.


2020 ◽  
Author(s):  
Callum Foden ◽  
Saidul Islam ◽  
Christian Arturo Fernandez Garcia ◽  
Leonardo Maugeri ◽  
Tom Sheppard ◽  
...  

<div>Peptides and the proteinogenic α-amino acids are essential to all life on Earth. Peptide biosynthesis is orchestrated by a complex suite of enzymes in extant biology, but this must have been predated by a simple chemical synthesis at the origins of life. α-Aminonitriles, the nitrile precursors of α-amino acids, are generally readily produced by Strecker reactions, but the origin of cysteine—the thiol-bearing amino acid—is not understood. The aminothiol moiety of cysteine is chemically incompatible with nitriles at physiological pH, therefore cysteine nitrile is not stable, and it is widely believed that cysteine was a biological invention and a late addition to the genetic code<sub>.</sub> Here, we report the first high-yielding, prebiotic synthesis of cysteine peptides. Our biomimetic synthesis converts serine to cysteine, by-passing the Strecker reaction of β-mercaptoacetaldehyde, but exploits nitrile–activated dehydroalanine synthesis at near-neutral pH. We additionally demonstrate the catalytic prowess of <i>N</i>-acylcysteines (and related peptides and thiols) in the organocatalytic synthesis of peptides and peptidyl amidines in neutral water. Thiol catalysis directly couples kinetically stable—but energy-rich—α-amidonitriles to proteinogenic amines, in a reaction that tolerates all twenty proteinogenic side chains. This is a rare, prebiotically plausible example of selective and efficient organocatalysis in water. Our results implicate cysteine derivatives and thiol-catalysis at the onset of evolution.</div>


2004 ◽  
Vol 11 (9) ◽  
pp. 1317-1324 ◽  
Author(s):  
Bing Hao ◽  
Gang Zhao ◽  
Patrick T. Kang ◽  
Jitesh A. Soares ◽  
Tsuneo K. Ferguson ◽  
...  

2011 ◽  
Vol 123 (27) ◽  
pp. 6261-6265 ◽  
Author(s):  
K. S. Ajish Kumar ◽  
Sudhir N. Bavikar ◽  
Liat Spasser ◽  
Tal Moyal ◽  
Shimrit Ohayon ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document