EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.99.10 | E120A | site-directed mutagenesis, the mutant has decreased deaminase activity in vitro, but retains the ability to complement ridA mutant phenotype | Salmonella enterica subsp. enterica serovar Typhimurium |
3.5.99.10 | R105A | site-directed mutagenesis, inactive mutant | Salmonella enterica subsp. enterica serovar Typhimurium |
3.5.99.10 | Y17F | site-directed mutagenesis, the mutant has decreased deaminase activity in vitro, but retains the ability to complement ridA mutant phenotype | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.99.10 | 2-aminoacrylate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminoacrylate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminoacrylate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminocrotonate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | - |
2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | - |
2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | - |
pyruvate + NH3 | - |
? | |
3.5.99.10 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | ? | - |
- |
|
3.5.99.10 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | ? | - |
- |
|
3.5.99.10 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | ? | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.99.10 | Salmonella enterica subsp. enterica serovar Typhimurium | Q7CP78 | - |
- |
3.5.99.10 | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | Q7CP78 | - |
- |
3.5.99.10 | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | Q7CP78 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.99.10 | 2-aminoacrylate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminoacrylate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminoacrylate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-aminocrotonate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | 2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | 2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | 2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminobutanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | 2-oxobutanoate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | pyruvate + NH3 | - |
? | |
3.5.99.10 | 2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | pyruvate + NH3 | - |
? | |
3.5.99.10 | additional information | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
- |
|
3.5.99.10 | additional information | proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
- |
|
3.5.99.10 | additional information | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | ? | - |
- |
|
3.5.99.10 | additional information | proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | ? | - |
- |
|
3.5.99.10 | additional information | addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA) | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | ? | - |
- |
|
3.5.99.10 | additional information | proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | ? | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.99.10 | reactive intermediate deaminase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
3.5.99.10 | ridA | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | General Information | Comment | Organism |
---|---|---|---|
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 | Salmonella enterica subsp. enterica serovar Typhimurium |
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 | Salmonella enterica subsp. enterica serovar Typhimurium |
3.5.99.10 | additional information | 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 | Salmonella enterica subsp. enterica serovar Typhimurium |
3.5.99.10 | physiological function | 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. Biological significance of enamine and imine production and importance of RidA in controlling the accumulation of reactive metabolites. The accumulation of enamines, specifically 2-aminoacrylate, can alter the physiological state of an organism, most notably through covalent damage of PLP-dependent enzymes. To that end, many organisms encode RidA, which facilitates the catalysis of enamines and imines in vivo. 2-Aminoacrylate produced by PLP-dependent alpha,beta-eliminases can be deaminated by RidA, with the PLP enzyme being both generator and target of 2-aminoacrylate | Salmonella enterica subsp. enterica serovar Typhimurium |