Issue 9, 2009

Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3)

Abstract

Active inclusion bodies of polyphosphate kinase 3 and cytidine 5′-monophosphate kinase were combined with whole cells that co-express sialic acid aldolase and CMP-sialic acid synthetase. The biocatalytic mixture was used for the synthesis of CMP-sialic acid, which was then converted to 3′-sialyllactose by whole cells.

Graphical abstract: Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3)

Supplementary files

Article information

Article type
Communication
Submitted
15 Dec 2008
Accepted
13 Mar 2009
First published
23 Mar 2009

Org. Biomol. Chem., 2009,7, 1778-1780

Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3)

J. Nahálka and V. Pätoprstý, Org. Biomol. Chem., 2009, 7, 1778 DOI: 10.1039/B822549B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements