3.5.99.10: 2-iminobutanoate/2-iminopropanoate deaminase
This is an abbreviated version!
For detailed information about 2-iminobutanoate/2-iminopropanoate deaminase, go to the full flat file.
Word Map on EC 3.5.99.10
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3.5.99.10
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enterica
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2-aminoacrylate
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pyridoxal
-
plp-dependent
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deaminases
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dehydratase
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5'-phosphate
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phosphoribosylamine
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lessons
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perchloric
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d-amino
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anthranilate
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branched-chain
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renamed
-
untargeted
-
5'-phosphate-dependent
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unchecked
-
acid-soluble
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thiamine
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archetypal
- 3.5.99.10
- enterica
- 2-aminoacrylate
- pyridoxal
-
plp-dependent
- deaminases
- dehydratase
- 5'-phosphate
-
phosphoribosylamine
-
lessons
-
perchloric
-
d-amino
- anthranilate
-
branched-chain
-
renamed
-
untargeted
-
5'-phosphate-dependent
-
unchecked
-
acid-soluble
- thiamine
-
archetypal
Reaction
Synonyms
ACIAD3089, AtRidA, enamine/imine deaminase, endoribonuclease L-PSP family protein, imine deaminase, PA0814, PA5083, PFL_1385, PSPTO_0102, PSPTO_3006, reactive intermediate deaminase, reactive intermediate deaminase A, Rid1, Rid2, Rid3, ridA, ST0811, yjgF, YjgF_endoribonc domain-containing protein
ECTree
3.5.99.10 2-iminobutanoate/2-iminopropanoate deaminaseAdvanced search results
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General Information on EC 3.5.99.10 - 2-iminobutanoate/2-iminopropanoate deaminase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
the ridA gene of Escherichia coli is indirectly regulated by BglG through the transcriptional regulator Lrp in stationary phase
physiological function
additional information
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
evolution
RidA forms the trimeric, barrel-like quaternary structure and intersubunit cavities, and resembles most RidA family members
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
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
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
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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
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)
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)
-
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
-
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)
-
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
-
physiological function
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
physiological function
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
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)
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
physiological function
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
physiological function
Pseudomonas aeruginosa strain PAO1 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)
physiological function
Pseudomonas fluorescens strain ATCC BAA-477 enzyme Rid3 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)
physiological function
Pseudomonas syringae pv. tomato 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)
physiological function
Pseudomonas syringae pv. tomato enzyme Rid3 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)
physiological function
reactive metabolites of enamine/imine nature generated during the breakdown of amino acids like serine and threonine are highly nucleophilic and pose a serious threat to cell viability. RidA deaminates these metabolites and facilitates their conversion into utilizable products, thus preventing cellular damage. Overexpression of ridA in Bgl+ background during stationary phase is physiologically relevant to eliminate toxic metabolites generated by the catabolism of serine-containing peptides as a result of elevated levels of their uptake
physiological function
RidA is an important enzyme for the prevention of toxic side products. By deaminating the toxic enamine/imine intermediates, it prevents the inactivation of many functionally important pyridoxal 5'-phosphate (PLP)-containing enzymes in plants such as branched-chain aminotransferase BCAT (IlvE). By converting the reactive enamine/imines to harmless 2-oxoacids, RidA preempts damage to BCAT3 and ensures that the isoleucine biosynthesis can proceed
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas fluorescens strain ATCC BAA-477 enzyme Rid3 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)
-
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)
-
physiological function
-
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
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
-
physiological function
-
Pseudomonas fluorescens strain ATCC BAA-477 enzyme Rid3 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas syringae pv. tomato enzyme Rid3 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)
-
physiological function
-
Pseudomonas syringae pv. tomato 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)
-
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
-
physiological function
-
Pseudomonas syringae pv. tomato enzyme Rid3 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)
-
physiological function
-
Pseudomonas syringae pv. tomato 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 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)
-
physiological function
-
Pseudomonas aeruginosa strain PAO1 enzyme Rid1 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)
-
physiological function
-
Pseudomonas fluorescens strain ATCC BAA-477 enzyme Rid3 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)
-
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
additional information
two serine residues, S80 and S92 are involved in hydrogen-bonding interactions with the backbone nitrogens of S162 and R165 respectively
additional information
-
two serine residues, S80 and S92 are involved in hydrogen-bonding interactions with the backbone nitrogens of S162 and R165 respectively
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
-
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
-
