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Literature summary extracted from

  • Hodge-Hanson, K.M.; Downs, D.M.
    Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro (2017), PLoS ONE, 12, e0185544 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.99.10 gene ACIAD3089, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Acinetobacter baylyi
3.5.99.10 gene PA0814, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Pseudomonas aeruginosa
3.5.99.10 gene PA5083, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Pseudomonas aeruginosa
3.5.99.10 gene PFL_1385, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Pseudomonas fluorescens
3.5.99.10 gene PSPTO_0102, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Pseudomonas syringae pv. tomato
3.5.99.10 gene PSPTO_3006, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 Pseudomonas syringae pv. tomato
3.5.99.10 gene ridA, overexpression in Escherichia coli strain BL21AI Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

EC Number Protein Variants Comment Organism
3.5.99.10 additional information the ridA-deficient mutant of Salmonella enterica strain DM12920 can be complemented by Rid family enzymes from Pseudomonas aeruginosa strain PAO1 (Rid1 and Rid2), Acinetobacter baylyi strain ATCC 33305 (Rid2), Pseudomonas syringae pv. tomato strain ATCC BAA-871 (Rid2 and Rid3), Pseudomonas fluorescens strain ATCC BAA-477 (Rid3), and by ridA from the Salmonella enterica wild-type LT2 Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.99.10 2-iminopropanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Acinetobacter baylyi
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas syringae pv. tomato
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas fluorescens
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa ATCC 15692
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas fluorescens Pf-5
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Acinetobacter baylyi BD413
-
 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 Pseudomonas fluorescens ATCC BAA-477
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa 1C
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas syringae pv. tomato DC3000
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas syringae pv. tomato ATCC BAA-871
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa PRS 101
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa DSM 22644
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa CIP 104116
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa LMG 12228
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Acinetobacter baylyi ATCC 33305
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas aeruginosa JCM 14847
-
 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O Pseudomonas fluorescens NRRL B-23932
-
 pyruvate + NH3
-
 ?
3.5.99.10 additional information Salmonella enterica subsp. enterica serovar Typhimurium the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Acinetobacter baylyi the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas syringae pv. tomato the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas fluorescens the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa ATCC 15692 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas fluorescens Pf-5 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Acinetobacter baylyi BD413 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas fluorescens ATCC BAA-477 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa 1C the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas syringae pv. tomato DC3000 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas syringae pv. tomato ATCC BAA-871 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa PRS 101 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa DSM 22644 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa CIP 104116 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa LMG 12228 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Acinetobacter baylyi ATCC 33305 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas aeruginosa JCM 14847 the enzyme reduces semicarbazone formation ?
-
-
3.5.99.10 additional information Pseudomonas fluorescens NRRL B-23932 the enzyme reduces semicarbazone formation ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.4.99.6 Pseudomonas aeruginosa
-
-
-
3.5.99.10 Acinetobacter baylyi Q6F828
-
-
3.5.99.10 Acinetobacter baylyi ATCC 33305 Q6F828
-
-
3.5.99.10 Acinetobacter baylyi BD413 Q6F828
-
-
3.5.99.10 Pseudomonas aeruginosa Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa 1C Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa 1C Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa ATCC 15692 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa ATCC 15692 Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa CIP 104116 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa CIP 104116 Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa DSM 22644 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa DSM 22644 Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa JCM 14847 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa JCM 14847 Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa LMG 12228 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa LMG 12228 Q9I5C5
-
-
3.5.99.10 Pseudomonas aeruginosa PRS 101 Q9HUA0
-
-
3.5.99.10 Pseudomonas aeruginosa PRS 101 Q9I5C5
-
-
3.5.99.10 Pseudomonas fluorescens Q4KGW9
-
-
3.5.99.10 Pseudomonas fluorescens ATCC BAA-477 Q4KGW9
-
-
3.5.99.10 Pseudomonas fluorescens NRRL B-23932 Q4KGW9
-
-
3.5.99.10 Pseudomonas fluorescens Pf-5 Q4KGW9
-
-
3.5.99.10 Pseudomonas syringae pv. tomato Q880Z0
-
-
3.5.99.10 Pseudomonas syringae pv. tomato Q88BB5
-
-
3.5.99.10 Pseudomonas syringae pv. tomato ATCC BAA-871 Q880Z0
-
-
3.5.99.10 Pseudomonas syringae pv. tomato ATCC BAA-871 Q88BB5
-
-
3.5.99.10 Pseudomonas syringae pv. tomato DC3000 Q880Z0
-
-
3.5.99.10 Pseudomonas syringae pv. tomato DC3000 Q88BB5
-
-
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
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.10 2-iminopropanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Acinetobacter baylyi pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas syringae pv. tomato pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas fluorescens pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa ATCC 15692 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas fluorescens Pf-5 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Acinetobacter baylyi BD413 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
-
 Pseudomonas fluorescens ATCC BAA-477 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa 1C pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas syringae pv. tomato DC3000 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas syringae pv. tomato ATCC BAA-871 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa PRS 101 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa DSM 22644 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa CIP 104116 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa LMG 12228 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Acinetobacter baylyi ATCC 33305 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas aeruginosa JCM 14847 pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pseudomonas fluorescens NRRL B-23932 pyruvate + NH3
-
 ?
3.5.99.10 additional information the enzyme reduces semicarbazone formation Salmonella enterica subsp. enterica serovar Typhimurium ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Acinetobacter baylyi ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas syringae pv. tomato ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas fluorescens ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Salmonella enterica subsp. enterica serovar Typhimurium ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas syringae pv. tomato ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas fluorescens ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Acinetobacter baylyi ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa ATCC 15692 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa ATCC 15692 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa ATCC 15692 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas fluorescens Pf-5 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas fluorescens Pf-5 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Acinetobacter baylyi BD413 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Acinetobacter baylyi BD413 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas fluorescens ATCC BAA-477 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas fluorescens ATCC BAA-477 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa 1C ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa 1C ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa 1C ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas syringae pv. tomato DC3000 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas syringae pv. tomato DC3000 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas syringae pv. tomato ATCC BAA-871 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas syringae pv. tomato ATCC BAA-871 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa PRS 101 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa PRS 101 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa PRS 101 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa DSM 22644 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa DSM 22644 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa DSM 22644 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa CIP 104116 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa CIP 104116 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa CIP 104116 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa LMG 12228 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa LMG 12228 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa LMG 12228 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Acinetobacter baylyi ATCC 33305 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Acinetobacter baylyi ATCC 33305 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas aeruginosa JCM 14847 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas aeruginosa JCM 14847 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA Pseudomonas aeruginosa JCM 14847 ?
-
-
3.5.99.10 additional information the enzyme reduces semicarbazone formation Pseudomonas fluorescens NRRL B-23932 ?
-
-
3.5.99.10 additional information enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA Pseudomonas fluorescens NRRL B-23932 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.4.99.6 DauA
-
 Pseudomonas aeruginosa
3.5.99.10 ACIAD3089
-
 Acinetobacter baylyi
3.5.99.10 endoribonuclease L-PSP family protein UniProt Pseudomonas syringae pv. tomato
3.5.99.10 endoribonuclease L-PSP family protein UniProt Pseudomonas fluorescens
3.5.99.10 imine deaminase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.5.99.10 imine deaminase
-
 Pseudomonas aeruginosa
3.5.99.10 imine deaminase
-
 Acinetobacter baylyi
3.5.99.10 imine deaminase
-
 Pseudomonas syringae pv. tomato
3.5.99.10 imine deaminase
-
 Pseudomonas fluorescens
3.5.99.10 PA0814
-
 Pseudomonas aeruginosa
3.5.99.10 PA5083
-
 Pseudomonas aeruginosa
3.5.99.10 PFL_1385
-
 Pseudomonas fluorescens
3.5.99.10 PSPTO_0102
-
 Pseudomonas syringae pv. tomato
3.5.99.10 PSPTO_3006
-
 Pseudomonas syringae pv. tomato
3.5.99.10 Rid1
-
 Pseudomonas aeruginosa
3.5.99.10 Rid2
-
 Pseudomonas aeruginosa
3.5.99.10 Rid2
-
 Acinetobacter baylyi
3.5.99.10 Rid2
-
 Pseudomonas syringae pv. tomato
3.5.99.10 Rid3
-
 Pseudomonas syringae pv. tomato
3.5.99.10 Rid3
-
 Pseudomonas fluorescens
3.5.99.10 ridA
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.5.99.10 YjgF_endoribonc domain-containing protein UniProt Pseudomonas aeruginosa
3.5.99.10 YjgF_endoribonc domain-containing protein UniProt Acinetobacter baylyi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.99.10 37
-
 in vivo assay at Salmonella enterica subsp. enterica serovar Typhimurium
3.5.99.10 37
-
 in vivo assay at Pseudomonas aeruginosa
3.5.99.10 37
-
 in vivo assay at Acinetobacter baylyi
3.5.99.10 37
-
 in vivo assay at Pseudomonas syringae pv. tomato
3.5.99.10 37
-
 in vivo assay at Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.99.10 8.7
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
3.5.99.10 8.7
-
 assay at Pseudomonas aeruginosa
3.5.99.10 8.7
-
 assay at Acinetobacter baylyi
3.5.99.10 8.7
-
 assay at Pseudomonas syringae pv. tomato
3.5.99.10 8.7
-
 assay at Pseudomonas fluorescens

General Information

EC Number General Information Comment Organism
1.4.99.6 physiological function proteins from the Rid2 and Rid3 subfamilies deaminate iminoarginine, generated in situ by D-arginine dehydrogenase DauA. DauA uses either a Rid protein or solvent water to generate a ketoacid. Rid proteins compete with semicarbazide for the iminoarginine product of the first reaction step Pseudomonas aeruginosa
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 Salmonella enterica subsp. enterica serovar Typhimurium
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 Pseudomonas aeruginosa
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 Acinetobacter baylyi
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 Pseudomonas syringae pv. tomato
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 Pseudomonas fluorescens
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) Salmonella enterica subsp. enterica serovar Typhimurium
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) Acinetobacter baylyi
3.5.99.10 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) Pseudomonas aeruginosa
3.5.99.10 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) Pseudomonas aeruginosa
3.5.99.10 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) Pseudomonas fluorescens
3.5.99.10 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) Pseudomonas syringae pv. tomato
3.5.99.10 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) Pseudomonas syringae pv. tomato