229171-29-3Relevant academic research and scientific papers
Chemoenzymatic Synthesis of Acyl Coenzyme A Substrates Enables in Situ Labeling of Small Molecules and Proteins
Agarwal, Vinayak,Diethelm, Stefan,Ray, Lauren,Garg, Neha,Awakawa, Takayoshi,Dorrestein, Pieter C.,Moore, Bradley S.
, p. 4452 - 4455 (2015/09/28)
A chemoenzymatic approach to generate fully functional acyl coenzyme A molecules that are then used as substrates to drive in situ acyl transfer reactions is described. Mass spectrometry based assays to verify the identity of acyl coenzyme A enzymatic products are also illustrated. The approach is responsive to a diverse array of carboxylic acids that can be elaborated to their corresponding coenzyme A thioesters, with potential applications in wide-ranging chemical biology studies that utilize acyl coenzyme A substrates.
Aminoacyl-coenzyme A synthesis catalyzed by a CoA ligase from Penicillium chrysogenum
Koetsier, Martijn J.,Jekel, Peter A.,Wijma, Hein J.,Bovenberg, Roel A.L.,Janssen, Dick B.
experimental part, p. 893 - 898 (2012/03/12)
Coenzyme A ligases play an important role in metabolism by catalyzing the activation of carboxylic acids. In this study we describe the synthesis of aminoacyl-coenzyme As (CoAs) catalyzed by a CoA ligase from Penicillium chrysogenum. The enzyme accepted medium-chain length fatty acids as the best substrates, but the proteinogenic amino acids l-phenylalanine and l-tyrosine, as well as the non-proteinogenic amino acids d-phenylalanine, d-tyrosine and (R)- and (S)-β-phenylalanine were also accepted. Of these amino acids, the highest activity was found for (R)-β-phenylalanine, forming (R)-β-phenylalanyl-CoA. Homology modeling suggested that alanine 312 is part of the active site cavity, and mutagenesis (A312G) yielded a variant that has an enhanced catalytic efficiency with β-phenylalanines and d-α-phenylalanine.
Stereospecific synthesis of threo- and erythro-β-hydroxyglutamic acid during kutzneride biosynthesis
Strieker, Matthias,Nolan, Elizabeth M.,Walsh, Christopher T.,Marahiel, Mohamed A.
supporting information; experimental part, p. 13523 - 13530 (2010/02/16)
The antifungal and antimicrobial kutznerides, hexadepsipeptides composed of one α-hydroxy acid and five nonproteinogenic amino acids, are remarkable examples of the structural diversity found in nonribosomally produced natural products. They contain D-3-h
