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Information on EC 3.5.99.10 - 2-iminobutanoate/2-iminopropanoate deaminase and Organism(s) Escherichia coli and UniProt Accession P0AF93

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IUBMB Comments
This enzyme, which has been found in all species and tissues examined, 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.
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Escherichia coli
UNIPROT: P0AF93
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
reactive intermediate deaminase, enamine/imine deaminase, atrida, imine deaminase, st0811, 2-iminobutanoate/2-iminopropanoate deaminase, reactive intermediate deaminase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-iminobutanoate aminohydrolase
This enzyme, which has been found in all species and tissues examined, 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two Bgl- strains ZK819-Tn10 and ZK819-Tn5 are isogenic derivatives of a common Bgl- parent strain ZK819 differing only in their antibiotic resistance markers that have been verified to be neutral. The two Bgl+ strains ZK819-97T and ZK819-bglR::IS1 have also been derived from the same Bgl- parent strain ZK819. The two strains differ only in the nature of the mutation that activates the operon. While ZK819-97T carries a point mutation in the CAP-cAMP binding site of the operon, ZK819-bglR::IS1 carries an IS1 insertion in the bglR regulatory region that activates the operon
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
the ridA gene of Escherichia coli is indirectly regulated by BglG through the transcriptional regulator Lrp in stationary phase
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ridA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21, quantitative expression analysis in Bgl- and Bgl+ strain ZK819 derivatives, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
leucine antagonizes the activation by inducing transcriptional factor Lrp
the ridA gene of Escherichia coli is indirectly regulated by BglG through the transcriptional regulator Lrp in stationary phase. Gene ridA is positively regulated by leucine responsive regulatory protein (Lrp) and leucine antagonizes the activation by Lrp, putative Lrp binding site within the ridA promoter. Purified Lrp protein binds to ridA promoter in vitro
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shukla, S.; Mahadevan, S.
The ridA gene of E. coli is indirectly regulated by BglG through the transcriptional regulator Lrp in stationary phase
Microbiology
165
683-696
2019
Escherichia coli (P0AF93), Escherichia coli
Manually annotated by BRENDA team