Any feedback?
Literature summary extracted from
- Expression of the DisA amino acid decarboxylase from Proteus mirabilis inhibits motility and class 2 flagellar gene expression in Escherichia coli (2013), Res. Microbiol., 164, 31-37.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.53 | Proteus mirabilis | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.53 | disA | - |
Proteus mirabilis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.1.53 | physiological function | enzyme expression in Escherichia coli blocks motility and results in a 50fold decrease in the expression of class 2 and class 3 flagellar genes fliA and fliC, respectively. The expression of flhDC encoding the class 1 activator of the flagellarcascade is unchanged by the expression at both the transcriptional and translational levels. Phenethylamine, a decarboxylation product derived from phenylalanine, is able to mimic the overexpression and decrease both motility and class 2/3 flagellar gene expression. Both enzyme overexpression and phenethylamine strongly inhibit biofilm formation in Escherichia coli. Enzyme overexpression and exogenous phenethylamine can also reduce motility in other enteric bacteria, but have no effect on motility in non-enteric Gram-negative bacteria | Proteus mirabilis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
