BioChem - DOS

Improved one-pot multienzyme (OPME) systems for synthesizing UDP-uronic acids and glucuronides

Chemical communications : Chem comm

Muthana, Musleh M.; Qu, Jingyao; Xue, Mengyang; Klyuchnik, Timofey; Siu, Alex; Li, Yanhong; Zhang, Lei; Yu, Hai; Li, Lei; Wang, Peng G.; Chen, Xi

<P><I>Arabidopsis thaliana</I> glucuronokinase (AtGlcAK) was cloned and shown to be able to use various uronic acids as substrates to produce the corresponding uronic acid-1-phosphates. AtGlcAK or <I>Bifidobacterium infantis</I> galactokinase (BiGalK) was used with a UDP-sugar pyrophosphorylase, an inorganic pyrophosphatase, with or without a glycosyltransferase for highly efficient synthesis of UDP-uronic acids and glucuronides. These improved cost-effective one-pot multienzyme (OPME) systems avoid the use of nicotinamide adenine dinucleotide (NAD<SUP>+</SUP>)-cofactor in dehydrogenase-dependent UDP-glucuronic acid production processes and can be broadly applied for synthesizing various glucuronic acid-containing molecules.</P><BR><BR><P>Graphic Abstract</P><P>Efficient one-pot multienzyme (OPME) systems were established for the synthesis of UDP-GlcA, UDP-GalA, and glucuronides from simple monosaccharides.<BR><IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c4cc10306h'><BR></P>

2015

The Royal Society of Chemistry

1359-7345

1364-548x

51

22

pp.4595-4598

10.1039/c4cc10306h

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART71597918

https://europepmc.org/articles/pmc4348237?pdf=render