Substrate promiscuities of a bacterial galactokinase and a glucose-1-phosphate uridyltransferase enable xylose salvaging-Reference-Cited by-同舟云学术

Substrate promiscuities of a bacterial galactokinase and a glucose-1-phosphate uridyltransferase enable xylose salvaging

Published:2022 Issue:9 Volume:24 Page:3717-3722
ISSN:1463-9262
Container-title:Green Chemistry
language:en
Short-container-title:Green Chem.

Author:

Shi Jin-Min¹^ORCID,Wu Ting-Ting¹,Zhou Hui¹,Zhang Yao-Yao¹,Liu Li¹^ORCID,Widmalm Göran²^ORCID,Voglmeir Josef¹^ORCID

Affiliation:

1. Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology Nanjing Agricultural University, 1 Weigang, 210095 Nanjing, China

2. Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden

Abstract

A bacterial galactokinase (ScGalK) phosphorylates xylose to xylose 1-phosphate, and allows xylose recycling via a simple UDP-xylose 'salvage pathway', which significantly reduces cofactor requirements compared to the known pentose phosphate pathway.

Funder

Vetenskapsrådet

Knut och Alice Wallenbergs Stiftelse

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Pollution,Environmental Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/GC/D2GC00657J

Reference27 articles.

1. Multifaceted roles of glycolytic enzymes