Structural highlights
Function
GUDB_BACSU GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Belitsky BR, Sonenshein AL. Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol. 1998 Dec;180(23):6298-305. PMID:9829940
- ↑ Commichau FM, Gunka K, Landmann JJ, Stulke J. Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system. J Bacteriol. 2008 May;190(10):3557-64. doi: 10.1128/JB.00099-08. Epub 2008 Mar 7. PMID:18326565 doi:http://dx.doi.org/10.1128/JB.00099-08