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Literature summary for 3.5.99.10 extracted from

  • Borchert, A.J.; Ernst, D.C.; Downs, D.M.
    Reactive enamines and imines in vivo lessons from the RidA paradigm (2019), Trends Biochem. Sci., 44, 849-860 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.99.10

Protein Variants

Protein Variants Comment Organism
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
R105A site-directed mutagenesis, inactive mutant Salmonella enterica subsp. enterica serovar Typhimurium
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-aminoacrylate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 pyruvate + NH3
-
 ?
2-aminoacrylate + H2O Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
 pyruvate + NH3
-
 ?
2-aminoacrylate + H2O Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
 pyruvate + NH3
-
 ?
2-aminocrotonate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
 2-oxobutanoate + NH3
-
 ?
2-iminopropanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 pyruvate + NH3
-
 ?
2-iminopropanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
 pyruvate + NH3
-
 ?
2-iminopropanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
 pyruvate + NH3
-
 ?
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) ?
-
-
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) ?
-
-
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) ?
-
-

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium Q7CP78
-
-
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 Q7CP78
-
-
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 Q7CP78
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminoacrylate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium pyruvate + NH3
-
 ?
2-aminoacrylate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 pyruvate + NH3
-
 ?
2-aminoacrylate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 pyruvate + NH3
-
 ?
2-aminocrotonate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 2-oxobutanoate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium pyruvate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 pyruvate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 pyruvate + NH3
-
 ?
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 ?
-
-
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 ?
-
-
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 ?
-
-
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 ?
-
-
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 ?
-
-
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 ?
-
-

Synonyms

Synonyms Comment Organism
reactive intermediate deaminase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
ridA
-
 Salmonella enterica subsp. enterica serovar Typhimurium

General Information

General Information Comment Organism
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
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
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
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