Nucleoside Diphosphate-Sugar 4-Epimerases | Zendy

Der-Fong Fan | Zendy; David S. Feingold | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Nucleoside Diphosphate-Sugar 4-Epimerases

Author(s) -

Der-Fong Fan,

David S. Feingold

Publication year - 1970

Publication title -

plant physiology

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.46.4.592

Subject(s) - chemistry , xylose , arabinose , chromatography , uridine diphosphate , nicotinamide adenine dinucleotide , sephadex , biochemistry , nicotinamide adenine dinucleotide phosphate , enzyme , michaelis–menten kinetics , uridine , enzyme assay , nad+ kinase , fermentation , oxidase test , rna , gene

Uridine diphosphate (UDP)-arabinose 4-epimerase (EC 5.1.3.5) has been purified at least 20-fold from wheat germ by MnCl(2) treatment, (NH(4))(2)SO(4) fractionation, dialysis, and Sephadex and diethylaminoethyl cellulose column chromatography. The enzyme has no action on UDP-d-glucose, UDP-d-glucuronic acid, or TDP-d-glucose. The pH optimum is 8.0. Km values are 1.5 mM for UDP-d-xylose and 0.5 mm for UDP-l-arabinose. The equilibrium constant, K, for the reaction UDP-l-arabinose left arrow over right arrow UDP-d-xylose is 1.25. The enzyme is neither activated by nicotinamide adenine dinucleotide nor inhibited by reduced nicotinamide adenine dinucleotide. It is completely inhibited by p-chloromercuri-phenylsulfonate; the inhibition is reversed by cysteine.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research