Carbon-Phosphorus Lyase-the State of the Art.
Binding Sites
Catalysis
Crystallography, X-Ray
Escherichia coli
/ enzymology
Genes, Bacterial
Glycine
/ analogs & derivatives
Gram-Negative Bacteria
/ enzymology
Gram-Positive Bacteria
/ enzymology
Herbicides
/ chemistry
Inorganic Chemicals
/ chemistry
Ions
Lyases
/ chemistry
Metals
/ chemistry
Molecular Conformation
Multigene Family
Operon
Organophosphonates
/ chemistry
Oxidation-Reduction
Phosphates
/ chemistry
Phosphorous Acids
/ chemistry
Soil Microbiology
Substrate Specificity
Glyphosate
C-P bond
Carbon-phosphorus lyase complex
Pho regulon
Phosphonate degradation
Phosphonates
phn operon
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
received:
12
03
2019
accepted:
23
10
2019
pubmed:
4
12
2019
medline:
30
1
2021
entrez:
4
12
2019
Statut:
ppublish
Résumé
Organophosphonates are molecules that contain a very chemically stable carbon-phosphorus (C-P) bond. Microorganisms can utilize phosphonates as potential source of crucial elements for their growth, as developed several pathways to metabolize these compounds. One among these pathways is catalyzed by C-P lyase complex, which has a broad substrate specifity; therefore, it has a wide application in degradation of herbicides deposited in the environment, such as glyphosate. This multi-enzyme system accurately recognized in Escherichia coli and genetic studies have demonstrated that it is encoded by phn operon containing 14 genes (phnC-phnP). The phn operon is a member of the Pho regulon induced by phosphate starvation. Ability to degradation of phosphonates is also found in other microorganisms, especially soil and marine bacteria, that have homologous genes to those in E. coli. Despite the existence of differences in structure and composition of phn gene cluster, each of these strains contains phnGHIJKLM genes necessary in the C-P bond cleavage mechanism. The review provides a detailed description and summary of achievements on the C-P lyase enzymatic pathway over the last 50 years.
Identifiants
pubmed: 31792787
doi: 10.1007/s12010-019-03161-4
pii: 10.1007/s12010-019-03161-4
doi:
Substances chimiques
Herbicides
0
Inorganic Chemicals
0
Ions
0
Metals
0
Organophosphonates
0
Phosphates
0
Phosphorous Acids
0
Lyases
EC 4.-
carbon-phosphorus lyase
EC 4.99.-
Glycine
TE7660XO1C
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM