Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzyme responsible for the stimulation by ATP AND NADPH of light emission catalyzed by bacterial luciferase has been partially purified from extracts of the luminescent bacterium, Photobacterium phosphoreum. The stimulatory activity was found to be stabilized by high concentrations of mercaptoethanol, permitting it to be separated from luciferase into an active and stable form and enabling further characterization of its functional properties. The activity of the enzyme was shown to be dependent not only on ATP and NADPH but also on the presence of a long chain fatty acid, and was inhibited by the addition of NADH and horse liver alcohol dehydrogenase. The specificity for fatty acids, as measured by the stimulation of luciferase activity, had a very limited range, with maximal luminescence being obtained with myristic acid and lower responses being observed only with tridecanoic and pentadecanoic acid. These results provide evidence in vitro for an enzyme in bioluminescent bacteria that functions as a fatty acid reductase converting fatty acids to aldehydes which in turn can be utilized by luciferase in the light-emitting reaction.
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PMID:Evidence for a fatty acid reductase catalyzing the synthesis of aldehydes for the bacterial bioluminescent reaction. Resolution from luciferase and dependence on fatty acids. 57 25

Three alcohol dehydrogenase (ADH) genes have recently been characterized in the yeast Kluyveromyces lactis. We report on a fourth ADH in K. lactis (KADH II: KADH2* gene) which is highly similar to other ADHs in K. lactis and Saccharomyces cerevisiae. KADH II appears to be a cytoplasmic enzyme, and after expression of KADH2 in S. cerevisiae enzyme activity comigrated with a K. lactis ADH present in cells grown in glucose or in ethanol. KADH I was also expressed in S. cerevisiae and it comigrated with a major ADH species expressed under glucose growth conditions in K. lactis. The substrate specificities for KADH I and KADH II were shown to be more similar to that of SADH II than to SADH I. SADH I cannot efficiently utilize long chain alcohols, in contrast to other cytoplasmic yeast ADHs, presumably because of the presence of a methionine (residue 271) in its substrate binding cleft. A comparison of the DNA sequences of ADHs among K. lactis, S. cerevisiae and Schizosaccharomyces pombe suggests that the ancestral yeast species contained one cytoplasmic ADH. After divergence from S. pombe, the ADH in the ancestor to K. lactis and S. cerevisiae was duplicated, and one ADH became localized to the mitochondrion, presumably for the oxidative use of ethanol. Following the speciation of S. cerevisiae and K. lactis, the gene encoding the cytoplasmic ADH in S. cerevisiae duplicated, which resulted in the development of the SADH II protein as the primary oxidative enzyme in place of SADH III. In contrast, the K. lactis mitochondrial ADH duplicated to give rise to the highly expressed KADH3 and KADH4 genes, both of which may still play primary roles in oxidative metabolism. These data suggest that K. lactis and S. cerevisiae use different compartments for their metabolism of ethanol. Our results also indicate that the complex regulatory circuits controlling the glucose-repressible SADH2 in S. cerevisiae are a recent acquisition from regulatory networks used for the control of genes other than SADH2.
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PMID:Evolution of the alcohol dehydrogenase (ADH) genes in yeast: characterization of a fourth ADH in Kluyveromyces lactis. 158 17

The serum activity of alcohol dehydrogenase was determined in healthy controls and in patients with liver diseases. The mean activity in hepatoma (6.4 +/- 1.0U/L) was significantly higher (P less than 0.05) than the mean values in liver cirrhosis (2.7 +/- 0.5U/L); hepatitis (4.3 +/- 1.0U/L), obstructive jaundice (2.9 +/- 0.5U/L) and healthy controls (0.7 +/- 0.1U/L). Alcohol dehydrogenase purified by CM-cellulose chromatography from the sera of patients with hepatoma had a higher affinity for butanol long chain saturated and unsaturated alcohols than the purified enzyme from healthy controls. Similarly, hepatoma alcohol dehydrogenase oxidized ethanol very poorly (KM = 154 microM) when compared with that from healthy controls (KM = 40.2 microM). Hepatoma alcohol dehydrogenase was inhibited by pyrazole while those of other liver diseases and the healthy controls were not. These properties of serum alcohol dehydrogenase may prove useful in the early diagnosis of hepatoma since biochemical changes occur before morphological changes in the development of cancer.
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PMID:Properties of serum alcohol dehydrogenase in Nigerians with primary hepatoma. 166 17

Human liver class III alcohol dehydrogenase (chi chi-ADH) and glutathione dependent formaldehyde dehydrogenase are the same enzyme. The enzyme, chi chi-ADH, exhibits a kcat of 200 min-1 and a km of 4 microM for the oxidation of formaldehyde, but only in the presence of GSH. In the absence of GSH the enzyme is essentially inactive toward formaldehyde but very active toward long chain alcohols. Thus, as in the rat (Koivusalo, M., Baumann, M., and Uotila, L. (1989) FEBS Letters 257, 105-109), the class III alcohol dehydrogenase and the GSH dependent formaldehyde dehydrogenase are identical enzymes. S-Hydroxymethyl derivatives of 8-thiooctanoate and lipoate are also very active substrates. The activity is specific for class III alcohol dehydrogenase; neither the class I and II nor the horse EE, ES, and SS isozymes oxidize hemithiolacetals. o-Phenanthroline competitively inhibits both activities and the two substrate types compete with each other.
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PMID:Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme. 187 53

A new form of alcohol dehydrogenase, designated mu-alcohol dehydrogenase, was identified in surgical human stomach mucosa by isoelectric focusing and kinetic determinations. This enzyme was anodic to class I (alpha, beta, gamma) and class II (pi) alcohol dehydrogenases on agarose isoelectric focusing gels. The partially purified mu-alcohol dehydrogenase, specifically using NAD+ as cofactor, catalyzed the oxidation of aliphatic and aromatic alcohols with long chain alcohols being better substrates, indicating a barrel-shape hydrophobic binding pocket for substrate. mu-Alcohol dehydrogenase stood out in high Km values for both ethanol (18 mM) and NAD+ (340 microM) as well as in high Ki value (320 microM) for 4-methylpyrazole, a competitive inhibitor for ethanol. mu-Alcohol dehydrogenase may account for up to 50% of total stomach alcohol dehydrogenase activity and appeared to play a significant role in first-pass metabolism of ethanol in human.
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PMID:Identification of a human stomach alcohol dehydrogenase with distinctive kinetic properties. 209 48

In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (chi) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brian and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles omega-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidation of long chain fatty alcohols and omega-hydroxyfatty acids.
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PMID:Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain. 265 Aug 3

An NADPH-dependent aldehyde reductase was purified from rat brain microsomes to electrophoretic homogeneity. The purified enzyme had a molecular weight of 75,000 and reduced long chain fatty aldehydes such as octanal and hexadecanal with higher affinity (Km values of 0.21 mM and 0.03 mM, respectively) than for various artificial carbonyl compounds such as p-nitrobenzaldehyde and p-nitroacetophenone (Km values of 0.31 mM and 1.4 mM, respectively). The purified microsomal aldehyde reductase also showed NADPH-cytochrome c reductase activity, and it could not be distinguished from NADPH-cytochrome c reductase in molecular weight (75,000), chromatographic behavior, electrophoretic mobility, or immunological properties. The solubilized microsomal fraction treated with steapsin lost the reductase activity for hexadecanal but not that for cytochrome c. These results suggest that the aldehyde reductase in brain microsomes is identical to NADPH-cytochrome c reductase and that a hydrophobic portion of the NADPH-cytochrome c reductase is required for the reduction of hexadecanal.
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PMID:Characterization of microsomal NADPH-dependent aldehyde reductase from rat brain. 308 64

The rat eye fraction, including retina, pigment epithelium and choroid, contains an alcohol dehydrogenase (ADH) isoenzyme that is not present in rat liver. Starch gel electrophoresis of retina ADH shows an anodic band that can be visualized by activity staining, using either ethanol or pentanol as substrates. Ethanol is a poor substrate (Km: 336 mM, at pH 10.0) for the purified retina ADH which prefers long chain, 2-unsaturated and aromatic alcohols. The enzyme has a pH optimum of 10.0 for ethanol oxidation and it is inhibited by 4-methylpyrazole (KI: 10 microM). Electrophoretic and kinetic properties clearly differentiate the retina ADH from the hepatic cathodic ADH isoenzymes and from an anodic chi-ADH-like form that we have also detected in rat liver. At the pH and ethanol concentrations found "in vivo," retina ADH can oxidize ethanol to an appreciable extent. The subsequent production of acetaldehyde and redox change may be responsible for visual disorders during alcohol intoxication.
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PMID:Properties of rat retina alcohol dehydrogenase. 316 Mar 70

1. Two distinct classes of alcohol dehydrogenase (ADH) isozymes were purified from guinea pig liver. 2. While the two classes of isozymes have similar subunit weight and electrophoretic mobility on starch gel, they differ markedly in catalytic properties. 3. The class A ADH oxidizes rapidly, exhibits saturated kinetics with both primary and secondary alcohols and is inhibited very effectively by 4-methylpyrazole (Ki = 0.58 microM) and o-phenanthroline (I50 = 0.1 mM). 4. The class B isozyme does not oxidize secondary alcohols, exhibits saturated kinetics only with long chain primary alcohols and is less sensitive to the ADH inhibitors 4-methylpyrazole (Ki = 15 mM) and o-phenanthroline (I50 greater than 10 mM).
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PMID:Guinea pig liver alcohol dehydrogenase: isolation and characterization of two distinct classes of isozymes. 335 31

The kinetic characteristics of alcohol dehydrogenase class III have been studied using class III isoenzymes purified from human liver (X-ADH) and rat liver (ADH-2). Our results confirm that long chain primary alcohols and aldehydes are the best substrates, although some aromatic compounds can also be actively metabolized. Kinetic analysis suggests an ordered bibi mechanism for X-ADH. Ethanol can be oxidized by class III isoenzymes at high substrate concentration, but with a very slow rate. Thus, their contribution to physiological ethanol elimination is probably insignificant. The general properties of the class III isoenzymes isolated from different mammals by ourselves and other authors are discussed.
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PMID:Mammalian alcohol dehydrogenase: characteristics of class III isoenzymes. 342 75


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