Harry S. Prihar scite author profile

GDPmannose dehydrogenase (EC 1.1.1.132) in a mucoid strain of Pseudomonas aeruginosa isolated from a patient with cystic fibrosis was identified by demonstrating the NAD-linked formation of GDPmannuronate from GDPmannose mediated by a cell extract of the organism. Nonmucoid mutant strains did not contain GDPmannose dehydrogenase, which suggests that the enzyme is involved in the biosynthesis of alginate-like polysaccharide by P. aeruginosa.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Harry S. Prihar

Biosynthesis of heparin. Substrate specificity of heparosan N-sulfate D-glucuronosyl 5-epimerase.

Biosynthesis of heparin. Hydrogen exchange at carbon 5 of the glycuronosyl residues

A gas chromatographic method for the quantitative detemination of hexuronic acids in alginic acid

Loss of C‐5 hydrogen during oxidation of UDP‐D‐glucose by UDP‐D‐glucose dehydrogenase

GDPmannose dehydrogenase and biosynthesis of alginate-like polysaccharide in a mucoid strain of Pseudomonas aeruginosa

Contact Info

Product

Resources

About