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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is established that the hamster prefers to drink alcohol under free choice situations. A gender difference in alcohol preference by the hamster has also been reported. In the present investigation, the alcohol metabolizing enzymes of hamsters of both sexes were measured. The liver alcohol dehydrogenase and aldehyde dehydrogenase activities were similar in both genders. A weak stomach alcohol dehydrogenase activity was also detected at high ethanol concentration; moreover, the activity of this enzyme in the male hamsters was 22% higher than that in the females. The total alcohol dehydrogenase activity in the stomach was less than 0.5% of that in the liver. Such a low activity suggested that the enzyme was unlikely to play a significant role in explaining the gender difference on alcohol preference in the hamster.
Biochem Mol Biol Int 1995 Jan
PMID:Alcohol metabolizing enzymes in the liver and stomach of the hamster. 773 33

The two moulds, Alternaria alternata and Cladosporium herbarum, are recognized as major causes of fungal allergies. Cloning, sequencing and heterologous expression of the allergens of the two moulds is a necessary step in understanding fungal allergy and in the development of new and improved methods of diagnosis and therapy. The seven new mould allergens presented here represent four new allergen proteins: aldehyde dehydrogenase (ALDH), enolase, YCP4 (previously found as a Saccharomyces cerevisiae protein of unknown function), and the acidic ribosomal protein, P2. Three of them (ALDH, YCP4 and P2) were found to be allergens in both fungi, Alternaria and Cladosporium. All allergens found so far are cytoplasmic proteins and are rather well conserved in evolution even when comparing distant species. Most of the allergens have "household" functions (ALDH, enolase). One allergen (P2) is a homolog of a very highly conserved human lupus erythematodes (LE) antigen. None of the fungal allergens is clearly related to other known non-fungal allergens.
Mol Immunol 1995 Feb
PMID:Molecular cloning of major and minor allergens of Alternaria alternata and Cladosporium herbarum. 789 96

A rabbit antiserum developed against purified rat liver daunorubicin-binding protein of M(r) 54,000 (DNR-BP54) cross-reacted with a mouse protein of the same molecular weight. This protein was expressed in the liver and several other organs of mice. A series of tumors and cell lines tested for the presence of the protein were negative. By immunocytochemistry, we found that DNR-BP54 was abundantly expressed in the cytoplasm of normal hepatocytes but was expressed at much lower levels in urethane-induced mouse liver tumors. By immunoscreening of a mouse liver cDNA library, we cloned the cDNA coding for DNR-BP54 and we found that this protein is aldehyde dehydrogenase-2 (EC 1.2.1.3). This result was confirmed by the dehydrogenase activity found in pure preparations of DNR-BP54 from normal rat and mouse livers, assayed with acetaldehyde as substrate and NAD as cofactor. The enzyme activity was inhibited by daunorubicin. The inhibition was found to be competitive with respect to NAD.
Mol Pharmacol 1994 Nov
PMID:The daunorubicin-binding protein of Mr 54,000 is an aldehyde dehydrogenase and is down-regulated in mouse liver tumors and in tumor cell lines. 796 77

The relative contribution of the aldehyde dehydrogenase (EC 1.2.1.3, ALDH) and glutathione (GSH) conjugate system to the degradation of (E)-4-hydroxy-2-nonenal (4HN), a toxic breakdown product arising from lipid peroxidation, was investigated in rat liver. Significant increases in the contents of 4HN and hexanal (HA) and a decrease of ALDH but not alcohol dehydrogenase (EC 1.1.1.2, ADH) activity were recognized in rat liver following administration of carbon tetrachloride (3 ml/kg, p.o.). Hepatic ALDH activity was correlated with HA production (r = -0.82, P < 0.01) but not with 4HN. When lipid peroxidation was induced by t-butyl hydroperoxide, the ratio of HA to 4HN production in the liver of rats pretreated with the ALDH inhibitor, cyanamide (100 mg/kg, i.p.) was higher than that in controls, whereas the ratio was lower in the liver of rats pretreated with the glutathione-depleting agent, phorone (250 mg/kg, i.p.). These results suggest that 4HN in rat liver is metabolized by the GSH-conjugate system in preference to degradation by ALDH.
Biochem Mol Biol Int 1994 Mar
PMID:Effects of aldehyde dehydrogenase and glutathione on the degradation of (E)-4-hydroxy-2-nonenal and N-hexanal in rat liver. 803 11

The cytosolic (Class 1) aldehyde dehydrogenase (AlDH) from sheep liver has been crystallized in a form suitable for X-ray diffraction studies. The crystals, grown by vapour diffusion using 6.5 to 7.5% methoxypolyethylene glycol 5000 as precipitant, at pH 6.5, are orthorhombic with cell dimensions a = 80.7, b = 92.5, c = 151.6 A, space-group P2(1)2(1)2(1), and one dimer in the asymmetric unit. The crystals diffract to at least 2.8 A resolution. Although unmodified AlDH crystallized readily, a key factor in obtaining diffraction-quality crystals was the covalent attachment of an active site reporter group, provided by 3,4-dihydro-3-methyl-6-nitro-2H-1,3-benzoxazin-2-one.
J Mol Biol 1994 Aug 12
PMID:Crystallization and preliminary X-ray diffraction studies on cytosolic (class 1) aldehyde dehydrogenase from sheep liver. 805 64

It has previously been reported that retinaldehyde can be converted to retinoic acid by cytosolic aldehyde dehydrogenase (AHD-2) in liver extracts [Biochem. Pharmacol. 42: 1279-1285 (1991)]. To determine which enzyme(s) carried out this reaction in murine embryonic stem cells, two aldehyde dehydrogenases were cloned; the AHD-2 gene was cloned from a liver cDNA library, and a closely related gene, AHD-M1, was cloned from an embryonic F9 cell cDNA library by conserved oligonucleotide sequence screening. AHD-M1 contained an open reading frame of 1554 base pairs, which encoded 517 amino acids. The AHD-M1 gene encoded a protein with a putative amino acid sequence that was 94% and 97% identical to the mitochondrial aldehyde dehydrogenases of human and rat, respectively, and thus we have cloned the murine cDNA for this enzyme for the first time. The AHD-M1 cDNA was only 64% identical to AHD-2. Northern analysis showed that AHD-M1 mRNA was constitutively expressed in F9 and P19 embryonic teratocarcinoma stem cells and in AB1 embryonic stem cells. There was a 3-5-fold retinoic acid-associated increase in the amount of this mRNA during the differentiation of F9 cells into parietal endoderm. In contrast, we could not detect the expression of AHD-2 mRNA in AB1, P19, or F9 cells, even though the F9 cells could convert retinaldehyde to retinoic acid. When the AHD-M1 and AHD-2 cDNAs were inserted into the expression vector pSG5 and transfected into cultured COS cells, 3-5-fold and 100-fold increases, respectively, in the conversion of [3H]retinaldehyde to [3H]retinoic acid could be detected by high performance liquid chromatographic assay. We conclude that both enzymes are capable of converting retinaldehyde to retinoic acid in intact COS cells. AHD-2 is more active than AHD-M1 in this conversion, but AHD-2 is not the enzyme responsible for this conversion in F9 embryonic stem cells.
Mol Pharmacol 1994 Jul
PMID:Enzymatic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases. 805 62

Human corneal aldehyde dehydrogenase (designated ALDH3) was purified to homogeneity and characterised with respect to substrate specificity and inhibition by thiol reagents. The enzyme was present as a major soluble protein (5% of the total soluble protein) and was found to efficiently catalyse the oxidation of medium chain peroxidic aldehydes which may be found in the cornea. These findings are consistent with the proposal that ALDH3 plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea. Disulfiram did not inhibit this enzyme under the conditions used in this study, however p-hydroxymercuribenzoate rapidly inactivated the enzyme. Analysis of the proteins of the cornea and surrounding tissue indicated that in both the cow and the human, changes in the nature and quantity of soluble proteins occurred. Phenotype variants of the ALDH3 were apparent in a small Australian population.
Biochem Mol Biol Int 1993 Sep
PMID:Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic variation. 826 Sep 46

The subcellular localization of the aldehyde dehydrogenase activity from the ALDH (EC 1.2.1.3) enzyme has been studied in nutritionally manipulated Drosophila melanogaster adults from a wild (LRC) and an ADH-null (bAdhn4) strain. ALDH activities from ALDH or ADH (EC 1.1.1.1) enzymes were selectively inhibited by prefeeding respectively the flies sucrose solutions supplemented with either cyanamide or acetone respectively. ALDH, ADH (as a cytosolic marker) and succinate dehydrogenase (EC 1.3.9.1) (as a mitochondrial marker) activities were assayed in both the mitochondrial and cytosolic fractions isolated from flies subjected to each treatment. Total ALDH activity in the cytosolic fraction was found to be between five (ADH strain) and ten (ADH strain) times higher than that in the mitochondrial fraction. Prefeeding cyanamide resulted in a 64% (ADH strain) and a 90% (ADH strain) reduction of the cytosolic ALDH activity, whereas prefeeding acetone resulted in a 38% (ADH strain) reduction of this activity. Prefeeding both cyanamide and acetone resulted in a total inhibition of ALDH activity, which was also observed after an extended cyanamide treatment. In conclusion, our results support that, contrary to what occurs in larvae, in adults the ALDH activity from ALDH enzyme is mainly localized in the cytosolic fraction: about 85% in ADH+ and 90% in ADH- strains. Although larvae and adults use different ALDH activities to detoxify acetaldehyde (from ADH and ALDH enzymes, respectively) both of them are cytosolic. Reasons for these different uses are discussed in relation to the subcellular localization of ALDH activity.
Insect Biochem Mol Biol 1993 Jul
PMID:Aldehyde dehydrogenase (ALDH) activity in Drosophila melanogaster adults: evidence for cytosolic localization. 835 17

Ethanol is known to acutely inhibit glucose-stimulated glycogen deposition in skeletal muscles in the rat. This effect is selective for oxidative as opposed to non-oxidative muscles. This paper explores the biochemical basis for this selective impairment in muscle glycogen metabolism. 4-Methylpyrazole, a potent inhibitor of alcohol dehydrogenase, potentiated the ethanol-mediated impairment in glycogen deposition in oxidative muscles and was associated with abnormalities in glycogen deposition in non-oxidative muscles. By contrast, disulfiram, a potent inhibitor of aldehyde dehydrogenase had no effect on the ethanol-mediated impairment in glycogen deposition in both oxidative and non-oxidative muscles. The implication is that it is the ethanol molecule itself, and not one of its metabolites (acetaldehyde, acetate, excess NADH), that mediates the defect in glycogen metabolism.
Biochem Mol Biol Int 1993 May
PMID:The mechanism(s) of the alcohol-induced impairment in glycogen synthesis in oxidative skeletal muscles. 835 29

Expression of alternative nitrogenases in Azotobacter vinelandii is repressed by molybdenum. Two strains with Tn5 insertion mutations showed alternative nitrogenase-dependent diazotrophic growth in the presence of Mo. The mutations were in a region which contained four open reading frames (ORFs 1-4). The genetic structure and predicted products of ORFs 2, 3 and 4 are typical of the membrane-associated elements of the ATP-binding cassette (ABC) superfamily of transport systems. The products of ORF3 and ORF4 are homologous with the products of the Escherichia coli genes chlD and the partially sequenced chlJ, respectively, both of which are implicated in molybdenum transport. ORF1, which is in the relative position of bacterial permease genes commonly specifying periplasmic binding proteins, encodes a 29 kDa protein with a novel primary structure. It lacks a potential signal sequence, and its C-terminal half consists of a tandem repeat of a segment which is homologous with the M(r) 7 kDa molybdenum-pterin binding protein Mop from Clostridium pasteurianum. This suggests that a substituted pterin may be involved in the initial capture or early metabolism of molybdenum.
Mol Microbiol 1993 Feb
PMID:Characterization of genes involved in molybdenum transport in Azotobacter vinelandii. 838 83


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