Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (2S)-2-acetamido-4-aminobutanoate Identifier CHEBI:77587 Charge 0 Formula C6H12N2O3 InChIKeyhelp_outline SUUKRBBXVBJLSS-YFKPBYRVSA-N SMILEShelp_outline CC(=O)N[C@@H](CC[NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-2,4-diaminobutanoate Identifier CHEBI:58761 Charge 1 Formula C4H11N2O2 InChIKeyhelp_outline OGNSCSPNOLGXSM-VKHMYHEASA-O SMILEShelp_outline [NH3+]CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 180 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:40951 | RHEA:40952 | RHEA:40953 | RHEA:40954 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581(T).
Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G., Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D., Kunte H.J.
The halophilic γ-proteobacterium Halomonas elongata DSM 2581(T) thrives at high salinity by synthesizing and accumulating the compatible solute ectoine. Ectoine levels are highly regulated according to external salt levels but the overall picture of its metabolism and control is not well understoo ... >> More
The halophilic γ-proteobacterium Halomonas elongata DSM 2581(T) thrives at high salinity by synthesizing and accumulating the compatible solute ectoine. Ectoine levels are highly regulated according to external salt levels but the overall picture of its metabolism and control is not well understood. Apart from its critical role in cell adaptation to halophilic environments, ectoine can be used as a stabilizer for enzymes and as a cell protectant in skin and health care applications and is thus produced annually on a scale of tons in an industrial process using H. elongata as producer strain. This paper presents the complete genome sequence of H. elongata (4,061,296 bp) and includes experiments and analysis identifying and characterizing the entire ectoine metabolism, including a newly discovered pathway for ectoine degradation and its cyclic connection to ectoine synthesis. The degradation of ectoine (doe) proceeds via hydrolysis of ectoine (DoeA) to Nα-acetyl-L-2,4-diaminobutyric acid, followed by deacetylation to diaminobutyric acid (DoeB). In H. elongata, diaminobutyric acid can either flow off to aspartate or re-enter the ectoine synthesis pathway, forming a cycle of ectoine synthesis and degradation. Genome comparison revealed that the ectoine degradation pathway exists predominantly in non-halophilic bacteria unable to synthesize ectoine. Based on the resulting genetic and biochemical data, a metabolic flux model of ectoine metabolism was derived that can be used to understand the way H. elongata survives under varying salt stresses and that provides a basis for a model-driven improvement of industrial ectoine production. << Less
Environ. Microbiol. 13:1973-1994(2011) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
submitter: Friedhelm Pfeiffer