1.1.1.284 12-hydroxydodecanoic acid + glutathione + NAD+ best substrate for ADH3 1.1.1.284 formaldehyde + glutathione + NAD+ - 1.1.1.284 formaldehyde + glutathione + NAD+ inducible enzyme 1.1.1.284 formaldehyde + glutathione + NAD+ inducible enzyme, at least one function of the enzyme in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment 1.1.1.284 formaldehyde + glutathione + NAD+ enzyme is found only in methanol-grown cells and is absent in cells grown on ethanol or glucose as carbon source 1.1.1.284 formaldehyde + glutathione + NAD+ main enzymatic system responsible for the formaldehyde elimination 1.1.1.284 formaldehyde + glutathione + NAD+ enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde 1.1.1.284 formaldehyde + glutathione + NAD+ principal enzyme for biological formaldehyde oxidation 1.1.1.284 formaldehyde + glutathione + NAD+ enzyme is involved in methanol metabolism 1.1.1.284 formaldehyde + glutathione + NAD+ key enzyme of the dissimilatory pathway of the methanol metabolism 1.1.1.284 formaldehyde + glutathione + NAD+ the synthesis of the enzyme is induced by methanol and repressed by glucose 1.1.1.284 formaldehyde + glutathione + NAD+ enzyme of methanol dissimilation. When cells are grown on glucose, the enzyme is not detected during the exponential growth, but is formed in the late stationary phase without addition of methanol. Enzyme is synthesized during growth on sorbitol, glycerol, ribose and xylose 1.1.1.284 formaldehyde + glutathione + NAD+ key step of the methanol catabolism in yeast 1.1.1.284 formaldehyde + glutathione + NAD+ resistance to formaldehyde is attributed to detoxification by oxidation 1.1.1.284 formaldehyde + glutathione + NAD+ enzyme of the formaldehyde oxidation pathway via the linear sequence 1.1.1.284 formaldehyde + glutathione + NAD+ enzyme is not essential but enhances the resistance against formaldehyde 1.1.1.284 formaldehyde + glutathione + NAD+ key enzyme in formaldehyde metabolism in microorganisms 1.1.1.284 formaldehyde + glutathione + NAD+ the enzyme activity in increased in livers from cancer patients independent of alcohol drinking or nondrinking, with no significant differences between primary and metastatic tumors 1.1.1.284 formaldehyde + glutathione + NAD+ the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione 1.1.1.284 formaldehyde + NAD+ + glutathione multifunctional enzyme, ADH3 constitutes a key enzyme in the detoxification of endogenous and exogenous formaldehyde, formaldehyde is released during intracellular metabolism of endogenous compounds or xenobiotics, expression of ADH3 might thus fulfill a protective role against DNA damage resulting from formaldehyde sources, ADH3 itself catalyzes oxidative reactions which produce NADH, most importantly the oxidation of formaldehyde 1.1.1.284 additional information the enzyme may be involved in the detoxification of long-chain lipid peroxidation products 1.1.1.284 additional information FLD1 is involved in the detoxification of formaldehyde in methanol metabolism, and Fld1p coordinates the formaldehyde level in methanol-grown cells according to the methanol concentration on growth. FLD activity is mainly induced by methanol, and this induction is not completely repressed by glucose 1.1.1.284 additional information key enzyme required for the catabolism of methanol as a carbon source and certain primary amines, such as methylamine as nitrogen sources in methylotrophic yeasts. The expression of FLDH1 is strictly regulated and can be controlled at two expression levels by manipulation of the growth conditions. The gene is strongly induced under methylotrophic growth conditions. Moderate expression is obtained under conditions in which a primary amine, e.g. methylamine is used as nitrogen source 1.1.1.284 additional information the enzyme is essential for growth on methanol 1.1.1.284 additional information the enzyme plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione 1.1.1.284 additional information genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview 1.1.1.284 additional information alcohol dehydrogenase 3, ADH3, acts as S-nitrosylglutathione reductase catalyzing the NADH-dependent reduction of S-nitrosoglutathione to GSSG and NH3, but also shows detoxification of formaldehyde catalyzing the formation of S-formylglutathione from formaldehyde and GSH 1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO 1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO 1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO 1.1.1.284 S-(hydroxymethyl)glutathione + NAD(P)+ multifunctional enzyme, large active site pocket of enzyme entails special substrate specificities: short-chain alcohols are poor substrates, while medium-chain alcohols and particularly the glutathione adducts S-hydroxymethylglutathioneand S-nitrosoglutathione are efficiently converted, universal presence and structural conservation imply that ADH3 performs essential housekeeping functions in living organisms 1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ - 1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ essential role in formaldehyde detoxifcation 1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ the enzyme plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite 1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ - 1.1.1.284 S-nitrosoglutathione + NADH the enzyme provides a defense mechanism against nitrosative stress, enzymatic pathway that modulates the bioactivity and toxicity of NO 1.1.1.284 S-nitrosoglutathione + NADH - 1.1.1.284 S-nitrosoglutathione + NADH + H+ ADH3 can affect the transnitrosation equilibrium between S-nitrosoglutathione and S-nitrosated proteins, arguing for an important role in NO homeostasis 1.1.1.284 S-nitrosoglutathione + NADH + H+ - 1.1.1.284 S-nitrosoglutathione + NADPH + H+ -