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

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

Murine corneal aldehyde dehydrogenase has been purified to homogeneity and characterized with a range of aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit molecular weight of 59 KDa. and appears to prefer aldehyde products of lipid peroxidation as substrates. The enzyme constituted approximately 5% of the total soluble protein of mouse cornea. A dual role has been proposed for corneal aldehyde dehydrogenase in providing the eye with protection against UV-B light: by oxidizing aldehydes generated through light-induced lipid peroxidation; and by the direct absorption of UV-B light by the enzyme.
Biochem Mol Biol Int 1993 Jul
PMID:Purification and properties of murine corneal aldehyde dehydrogenase. 840 11

A 56 kDa protein expressed in human genital skin fibroblasts was first identified by independent laboratories on the basis of its specific expression in androgen target cells and its ability to covalently bind androgenic affinity ligands. Recently, immunoscreening of a cDNA library with antisera directed against this protein resulted in the isolation of a partial cDNA clone identical to human cytosolic aldehyde dehydrogenase (ALDH1). We report here the preparation of a full-length cDNA encoding ALDH1 from human genital fibroblasts. Translation of the encoded protein in a cell-free system yields a 56 kDa product that can be covalently radiolabeled with [3H]dihydrotestosterone 17 beta-bromoacetate (DHT-BA). Expression of the full-length clone in mammalian cells also results in expression of a 56 kDa DHT-BA binding protein. The covalent binding of DHT-BA by ALDH1 is an intrinsic property of the enzyme and is not dependent on androgen receptor expression.
Mol Cell Endocrinol 1993 Feb
PMID:An androgenic affinity ligand covalently binds to cytosolic aldehyde dehydrogenase from human genital skin fibroblasts. 847 48

Ethanol-utilization in Aspergillus nidulans is mediated by alcohol dehydrogenase I and aldehyde dehydrogenase encoded by alcA and aldA, respectively. Both genes are under the transcriptional control of the specific activator AlcR and the general carbon catabolite repressor CreA. The alcR and alcA genes are closely linked in chromosome VII; aldA is located in chromosome VIII. We have identified five other transcripts that are expressed from the same genomic region as alcA and alcR. They are inducible by the gratuitous inducer ethyl methyl ketone (EMK), and are carbon catabolite repressed. The corresponding genes, designated alcM, alcS, alcO, alcP, and alcU, are differentially regulated by the specific transcriptional activator AlcR, and they are not all under the direct control by the CreA repressor. Some of the inducible transcripts are very abundant in the cell, whereas others are poorly expressed. Two sets of genes, alcM/alcS and alcR/alcO, are divergently transcribed and probably share a common cis-acting region, whereas alcP and alcU are individually transcribed from the same strand as alcA and alcR, and have their own promoters. The significance of the alc gene clustering is discussed. At least four of the five novel alc genes in the cluster are not essential for ethanol metabolism.
Mol Microbiol 1996 May
PMID:A newly identified gene cluster in Aspergillus nidulans comprises five novel genes localized in the alc region that are controlled both by the specific transactivator AlcR and the general carbon-catabolite repressor CreA. 873 27

A locust within chromosome XIII of Saccharomyces cerevisiae containing four genes upregulated by osmotic stress has been characterized. Two of the genes, but not their osmotic induction, were already described: the DNA damage-inducible gene DDR48 and the protease inhibitor gene PAI3. The two novel genes encode a cytoplasmic aldehyde dehydrogenase (ALD2) and a peptide of unknown function (SIP18). These genes form a cluster of two pairs of divergent promoters regulated by osmotic stress. The regulation of the divergent ALD2 and DDR48 genes, however, occurs by different mechanisms. ALD2 exhibits maximum induction with 0.3 M NaCl, negative regulation by protein kinase A and dependence on PBS2 and HOG1 protein kinases for osmotic induction. DDR48 requires 1 M NaCl for maximum induction and its expression in independent of PBS2 and HOG1 protein kinases and less sensitive to protein kinase A. PAI3 and SIP18 are as dependent on the above protein kinases as ALD2. Deletion analysis indicates that most of the regulation of the ALD2 promoter is mediated by a negative element counteracted by osmotic stress.
Mol Microbiol 1995 Aug
PMID:A genomic locus in Saccharomyces cerevisiae with four genes up-regulated by osmotic stress. 880 20

The possible effect of several physiologically important aldehydes has been tested on partially purified glyoxalase I of Ehrlich ascites carcinoma (EAC) cells. The results indicate that D, and L-lactaldehyde are strong non-competitive inhibitors of glyoxalase I and the effect with the D-isomer is more pronounced, whereas both D,L-glyceraldehyde and acetaldehyde are moderately inhibitory and the nature of inhibition is strictly competitive. Moreover, D,L-glyceraldehyde strongly inhibits the utilization of methylglyoxal by intact EAC cells. A search for the presence of several aldehyde metabolizing enzymes in EAC cells indicates that non-specific aldehyde reductase, methylglyoxal reductase, aldehyde dehydrogenase and alcohol dehydrogenase are apparently absent in this rapidly growing, highly de-differentiated malignant cell.
Mol Cell Biochem 1996 Dec 06
PMID:Interaction of aldehydes with glyoxalase I and the status of several aldehyde metabolizing enzymes of Ehrlich ascites carcinoma cells. 897 76


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