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


ABSTRACT: Arabidopsis thaliana 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 Bifidobacterium infantis 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(+))-cofactor in dehydrogenase-dependent UDP-glucuronic acid production processes and can be broadly applied for synthesizing various glucuronic acid-containing molecules.

SUBMITTER: Muthana MM 

PROVIDER: S-EPMC4348237 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

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

Muthana Musleh M MM   Qu Jingyao J   Xue Mengyang M   Klyuchnik Timofey T   Siu Alex A   Li Yanhong Y   Zhang Lei L   Yu Hai H   Li Lei L   Wang Peng G PG   Chen Xi X  

Chemical communications (Cambridge, England) 20150301 22


Arabidopsis thaliana 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 Bifidobacterium infantis 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 n  ...[more]

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