In:
PLOS Biology, Public Library of Science (PLoS), Vol. 21, No. 9 ( 2023-9-21), p. e3002285-
Abstract:
The canonical glycolysis pathway is responsible for converting glucose into 2 molecules of acetyl-coenzyme A (acetyl-CoA) through a cascade of 11 biochemical reactions. Here, we have designed and constructed an artificial phosphoketolase (APK) pathway, which consists of only 3 types of biochemical reactions. The core enzyme in this pathway is phosphoketolase, while phosphatase and isomerase act as auxiliary enzymes. The APK pathway has the potential to achieve a 100% carbon yield to acetyl-CoA from any monosaccharide by integrating a one-carbon condensation reaction. We tested the APK pathway in vitro, demonstrating that it could efficiently catabolize typical C1-C6 carbohydrates to acetyl-CoA with yields ranging from 83% to 95%. Furthermore, we engineered Escherichia coli stain capable of growth utilizing APK pathway when glycerol act as a carbon source. This novel catabolic pathway holds promising route for future biomanufacturing and offering a stoichiometric production platform using multiple carbon sources.
Type of Medium:
Online Resource
ISSN:
1545-7885
DOI:
10.1371/journal.pbio.3002285
DOI:
10.1371/journal.pbio.3002285.g001
DOI:
10.1371/journal.pbio.3002285.g002
DOI:
10.1371/journal.pbio.3002285.g003
DOI:
10.1371/journal.pbio.3002285.g004
DOI:
10.1371/journal.pbio.3002285.s001
DOI:
10.1371/journal.pbio.3002285.s002
DOI:
10.1371/journal.pbio.3002285.s003
DOI:
10.1371/journal.pbio.3002285.s004
DOI:
10.1371/journal.pbio.3002285.s005
DOI:
10.1371/journal.pbio.3002285.s006
DOI:
10.1371/journal.pbio.3002285.s007
DOI:
10.1371/journal.pbio.3002285.s008
DOI:
10.1371/journal.pbio.3002285.s009
DOI:
10.1371/journal.pbio.3002285.s010
DOI:
10.1371/journal.pbio.3002285.s011
DOI:
10.1371/journal.pbio.3002285.s012
DOI:
10.1371/journal.pbio.3002285.s013
DOI:
10.1371/journal.pbio.3002285.s014
DOI:
10.1371/journal.pbio.3002285.s015
DOI:
10.1371/journal.pbio.3002285.s016
DOI:
10.1371/journal.pbio.3002285.s017
DOI:
10.1371/journal.pbio.3002285.s018
DOI:
10.1371/journal.pbio.3002285.s019
DOI:
10.1371/journal.pbio.3002285.s020
DOI:
10.1371/journal.pbio.3002285.s021
DOI:
10.1371/journal.pbio.3002285.s022
DOI:
10.1371/journal.pbio.3002285.s023
DOI:
10.1371/journal.pbio.3002285.s024
DOI:
10.1371/journal.pbio.3002285.s025
DOI:
10.1371/journal.pbio.3002285.s026
DOI:
10.1371/journal.pbio.3002285.s027
DOI:
10.1371/journal.pbio.3002285.s028
DOI:
10.1371/journal.pbio.3002285.s029
DOI:
10.1371/journal.pbio.3002285.s030
DOI:
10.1371/journal.pbio.3002285.s031
DOI:
10.1371/journal.pbio.3002285.s032
DOI:
10.1371/journal.pbio.3002285.s033
DOI:
10.1371/journal.pbio.3002285.s034
DOI:
10.1371/journal.pbio.3002285.s035
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2023
detail.hit.zdb_id:
2126773-X
Permalink