Putative metal-binding enzyme; Type II glyoxalase, isozyme of GloB, that hydrolyzes (R)-S- lactoylglutathione to (R)-lactate and glutathione. Plays a minor contribution to methylglyoxal (MG) detoxification in E.coli, compared to GloB. The two isoenzymes have additive effects and ensure maximal MG degradation.

Protein/nucleic acid deglycase 1; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, [...]

Chromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...]

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Aldehyde dehydrogenase A, NAD-linked; Acts on lactaldehyde as well as other aldehydes.

Glyoxylate/hydroxypyruvate reductase B; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2- keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D- fructose and L-sorbose. Activity with NAD is very low; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.

Glyoxylate/hydroxypyruvate reductase A; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low.

Tyramine oxidase, copper-requiring; The enzyme prefers aromatic over aliphatic amines; Belongs to the copper/topaquinone oxidase family.

Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine; Belongs to the TrpB family.