Biological synthesis of nicotinamide mononucleotide.
Enzymatic production
Nicotinamide mononucleotide
Nicotinamide phosphoribosyltransferase
Phosphoribosyl diphosphate
Journal
Biotechnology letters
ISSN: 1573-6776
Titre abrégé: Biotechnol Lett
Pays: Netherlands
ID NLM: 8008051
Informations de publication
Date de publication:
Dec 2021
Dec 2021
Historique:
received:
03
02
2021
accepted:
23
09
2021
pubmed:
10
10
2021
medline:
1
3
2022
entrez:
9
10
2021
Statut:
ppublish
Résumé
Nicotinamide mononucleotide (NMN) or Nicotinamide-1-ium-1-β-D-ribofuranoside 5'-phosphate is a nucleotide that can be converted into nicotinamide adenine dinucleotide (NAD) in human cells. NMN has recently attracted great attention because of its potential as an anti-aging drug, leading to great efforts for its effective manufacture. The chemical synthesis of NMN is a challenging task since it is an isomeric compound with a complicated structure. The majority of biological synthetic routes for NMN is through the intermediate phosphoribosyl diphosphate (PRPP), which is further converted to NMN by nicotinamide phosphoribosyltransferase (Nampt). There are various routes for the synthesis of PRPP from simple starting materials such as ribose, adenosine, and xylose, but all of these require the expensive phosphate donor adenosine triphosphate (ATP). Thus, an ATP regeneration system can be included, leading to diminished ATP consumption during the catalytic process. The regulations of enzymes that are not directly involved in the synthesis of NMN are also critical for the production of NMN. The aim of this review is to present an overview of the biological production of NMN with respect to the critical enzymes, reaction conditions, and productivity.
Identifiants
pubmed: 34626279
doi: 10.1007/s10529-021-03191-1
pii: 10.1007/s10529-021-03191-1
doi:
Substances chimiques
Cytokines
0
Nucleotides
0
NAD
0U46U6E8UK
Nicotinamide Mononucleotide
1094-61-7
Ribose
681HV46001
Adenosine Triphosphate
8L70Q75FXE
Xylose
A1TA934AKO
Nicotinamide Phosphoribosyltransferase
EC 2.4.2.12
nicotinamide phosphoribosyltransferase, human
EC 2.4.2.12
Adenosine
K72T3FS567
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2199-2208Subventions
Organisme : fundamental research funds for the central universities
ID : RF-C2020002
Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Nature B.V.
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