Novel catalytic property of fructose-6-phosphate aldolase in directly conversion of two 1-hydroxyalkanones to diketones.

Aldehyde-Lyases / metabolism Catalysis Escherichia coli / metabolism Fructose-Bisphosphate Aldolase / metabolism Fructosephosphates Ketones Substrate Specificity
Aldol condensation Aldolases Biocatalysis Hydroxyacetone

Journal

Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761

Informations de publication

Date de publication:
Jun 2021
Historique:
received: 03 01 2021
revised: 23 02 2021
accepted: 02 03 2021
entrez: 16 5 2021
pubmed: 17 5 2021
medline: 19 8 2021
Statut: ppublish

Résumé

Asymmetric CC bond formation catalyzed by aldolases requires the supplementation of nucleophiles and receptors in the reaction medium. However, aldol condensation using a single ketone as substrate has never been reported yet. In this work, we discovered that d-fructose-6-phosphate aldolase (FSA) could convert two 1-hydroxyalkanones, such as hydroxyacetone (HA) and 1-hydroxy-2-butanone, into two type of diketones. The initial product synthesis rate increased 3-fold and the yield reached to 56 %, when pure oxygen was directly inputted into the reaction medium. The results confirmed that oxygen participated in this reaction and hydrogen peroxide was generated. Metal ions Co

Identifiants

DOI: 10.1016/j.enzmictec.2021.109784 PMID: 33992412
pubmed: 33992412
pii: S0141-0229(21)00042-9
doi: 10.1016/j.enzmictec.2021.109784
pii:
doi:

Substances chimiques

Fructosephosphates 0
Ketones 0
fructose-6-phosphate 6814-87-5
Aldehyde-Lyases EC 4.1.2.-
Fructose-Bisphosphate Aldolase EC 4.1.2.13

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

109784

Informations de copyright

Copyright © 2021 Elsevier Inc. All rights reserved.

Auteurs

Chenxi Ren (C)

University of Chinese Academy of Sciences, Beijing, 100049, China; National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China.

Jiangang Yang (J)

National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China. Electronic address: yang_jg1@tib.cas.cn.

Yan Zeng (Y)

National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China.

Tong Zhang (T)

National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China.

Chaoyu Tian (C)

National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China.

Yan Men (Y)

National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China.

Yuanxia Sun (Y)

University of Chinese Academy of Sciences, Beijing, 100049, China; National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China; National Technology Innovation Center of Synthetic Biology, Tianjin 300308, China. Electronic address: sun_yx@tib.cas.cn.

Articles similaires

Bioinspired gelated cell sheet-supported lactobacillus biofilm for aerobic vaginitis diagnosis and treatment.

Yueyue Gui, Qingfei Sun, Kexin Li et al.
1.00
Female Biofilms Animals Lactobacillus Mice

Saccharomyces cerevisiae whole cell biotransformation for the production of aldehyde flavors and fragrances.

Nazreen V M Abdul Muthaliff, Yao Zong Ng, Wei Mei Guo et al.
1.00
Saccharomyces cerevisiae Aldehydes Biotransformation Flavoring Agents Lipoxygenase

Prediction of strain level phage-host interactions across the Escherichia genus using only genomic information.

Baptiste Gaborieau, Hugo Vaysset, Florian Tesson et al.
1.00
Host Specificity Bacteriophages Genomics Algorithms Escherichia coli

Mutational analysis of Phanerochaete chrysosporium´s purine transporter.

Mariana Barraco-Vega, Manuel Sanguinetti, Gabriela da Rosa et al.
1.00
Phanerochaete Fungal Proteins Purines Aspergillus nidulans DNA Mutational Analysis

Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Lyases › Carbon-carbon lyases › Aldehyde-lyases › Novel catalytic property of...
questionsmedicales.fr › Phénomènes chimiques › Catalyse › Novel catalytic property of...
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Enterobacteriaceae › Escherichia › Escherichia coli › Novel catalytic property of...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Lyases › Carbon-carbon lyases › Aldehyde-lyases › Fructose bisphosphate aldolase › Novel catalytic property of...
questionsmedicales.fr › Glucides › Oses phosphates › Hexose phosphate › Fructose phosphate › Novel catalytic property of...
questionsmedicales.fr › Composés chimiques organiques › Cétones › Novel catalytic property of...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Novel catalytic property of...