EC Number   |
General Information |
Reference |
|---|
   3.5.99.10 | evolution |
genetic and biochemical studies have outlined a role for the broadly conserved reactive intermediate deaminase (Rid) (YjgF/YER057c/UK114) protein family, in particular RidA, in catalyzing the hydrolysis of enamines and imines to their ketone product. Rid proteins are conserved in all domains of life and split into an archetypal RidA subfamily and seven other subfamilies (Rid1-Rid7). Rid4-Rid7 proteins are missing an active-site arginine essential for the enamine/imine deaminase activity seen in the other subfamilies, suggesting additional uncharacterized roles for Rid enzymes. R105 is absolutely conserved in RidA and Rid1-Rid3 subfamily members, predicting that members of these protein subfamilies act on amino acid-derived substrates. Furthermore, the Rid4-Rid7 subfamilies lack R105 and no amino acid-derived enamine/imine deaminase activity has been detected for these subfamilies |
-, 758515 |
| 3.5.99.10 | evolution |
RidA forms the trimeric, barrel-like quaternary structure and intersubunit cavities, and resembles most RidA family members |
758371 |
| 3.5.99.10 | evolution |
the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies |
-, 758158 |
| 3.5.99.10 | malfunction |
in the absence of RidA, 2-aminoacrylate accumulates and damages pyridoxal 5'-phosphate (PLP)-dependent enzymes through covalent modification. 2-Aminoacrylate (2AA) generated during these promiscuous elimination reactions can immediately and irreversibly damage the source PLP-dependent enzymes before 2AA escapes the active site. The irreversible inactivation could be caused by: (i) release of 2AA from PLP and subsequent nucleophilic attack of the electrophilic enzyme-bound PLP Schiff base by the beta-carbon of 2AA, or (ii) attack of the 2AA/PLP adduct by active site nucleophilic residues, detailed overview |
-, 758515 |
| 3.5.99.10 | malfunction |
loss of ridA function in a Bgl+ background results in a significant growth retardation in serine-containing media compared to that in a Bgl- background. Deletion of ridA is more disadvantageous in a Bgl+ background, complex metabolic phenotypes like sensitivity to serine in glucose-rich medium and inability to grow on pyruvate as the sole carbon source, overview |
757626 |
| 3.5.99.10 | malfunction |
Salmonella enterica strains lacking gene ridA have a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) |
-, 758158 |
| 3.5.99.10 | metabolism |
the ridA gene of Escherichia coli is indirectly regulated by BglG through the transcriptional regulator Lrp in stationary phase |
757626 |
| 3.5.99.10 | more |
proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Residue R105 is essential for catalytic activity. The backbone carbonyl groups of R105 and G31 appear to stabilize the iminium ion (e.g. 2-iminopropanoate) formed from the substrate, while the backbone of C107 and the side chain of Glu120 coordinate the water involved in hydrolysis of 2-iminopropanoate |
-, 758515 |
| 3.5.99.10 | more |
two serine residues, S80 and S92 are involved in hydrogen-bonding interactions with the backbone nitrogens of S162 and R165 respectively |
758371 |
| 3.5.99.10 | physiological function |
Acinetobacter baylyi strain ATCC 33305 enzyme Rid2 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) |
-, 758158 |
