dosP:Quickview
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
<protect>
| Standard Name |
dosP |
|---|---|
| Gene Synonym(s) |
ECK1483, b1489, JW1484, yddU, dos[1], dos, yddU |
| Product Desc. |
phosphodiesterase, heme-regulated[2][3]; Component of phosphodiesterase, heme-regulated[3] c-di-GMP phosphodiesterase, heme-regulated oxygen sensor; may have weak cAMP PDE activity; tetrameric[4] |
| Product Synonyms(s) |
cAMP phosphodiesterase, heme-regulated[1], B1489[2][1], YddU[2][1], DosP[2][1] , dos, ECK1483, JW1484, yddU, b1489 |
| Function from GO |
<GO_nr /> |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity | |
| Quick Links |
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Notes
YddV/Dos may constitute a cyclic-di-GMP synthesis/degradation module (Mendez-Ortiz, 2006). The EAL domain of Dos has been shown to be a c-di-GMP-specific phosphodiesterase and does not have cAMP phosphodiesterase activity, in contrast to an earlier report (Sasakura, 2002; Schmidt, 2005). cAMP hydrolysis by full length Dos found by Sasakura (2002) is three orders of magnitude slower than the rate of c-di-GMP hydrolysis, may not be physiologically relevant, and may be due to the use of 2'-O-anthraniloyl-cAMP instead of cAMP as substrate (Schmidt, 2005). Redox changes in the bound heme result in global 3D structural alterations; this "scissor-type" subunit movement aids in catalytic control. Dos contains 2 N-terminal heme binding PAS domains, a GGDEF domain, and a C-terminal EAL domain. The start codon might be 8 codons upstream. dos expression is elevated under aerobic conditions where it is partially responsible for cAMP degradation. The heme binding domain is called DosH. Asp40 is involved in the electronic structure of the haem iron and redox-dependent catalytic control of the PDE domain because mutations in Asp40 result in lack of catalytic activity. Second gene in yddV-dos operon. A dos mutant is reported to have elevated cAMP under aerobic conditions, but this may be an indirect effect or it may reflect a physiologically relevant cAMP PDE activity in vivo.[4]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
