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Query: UNIPROT:P06889 (Mol)
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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

The present study demonstrated a significant variation of liver aldehyde oxidase activity in twelve strains of rats. The highest activity was found with Sea:SD rats and the lowest one with WKA/Sea rats. When assayed using benzaldehyde as a substrate, the difference in the activity between the two strains was 63.5-fold. Little significant differences in Km values of the enzyme were observed among several strains. On the other hand, Western blot analysis for the enzyme suggested that the strains possess different quantities of the enzyme, which are roughly parallel to aldehyde oxidase activity observed in the strains.
Biochem Mol Biol Int 1995 Nov
PMID:Strain differences of liver aldehyde oxidase activity in rats. 862 91

The pathways participating in the metabolism of the nitrofuran antimicrobial drug N-[5-nitro-2-furfurylidene]-3-amino-2-oxazolidinone (furazolidone) in intact cells were investigated in the human intestinal cell line Caco-2. One-electron reduction of furazolidone led to the formation of a free radical intermediate that could be monitored in dense cell suspensions by noninvasive electron spin resonance spectroscopy. The effects of enzyme inhibitors on the kinetics of radical production and decay were used to estimate the relative contribution of different enzymes to the reductive activation of the drug. Although many enzymes are known to reduce nitrofurans in vitro (e.g., xanthine oxidase, aldehyde oxidase, DT-diaphorase, mitochondrial redox chain components), their contributions were insignificant in living Caco-2 cells. The first reducing equivalent required for the formation of the nitroanion derivative of furazolidone appeared to be provided essentially by the microsomal cytochrome P450 reductase. This was confirmed through studies of the NADPH-dependent radical formation by microsomes. Differentiated Caco-2 cells, an established enterocyte model, showed only modestly increased radical formation and the same enzyme-specificity pattern as undifferentiated cells. Consistently, only a small increase in P450 reductase activity was found in differentiated cells, in contrast to the 10-fold increase seen in typical differentiation marker enzymes. With the electron spin resonance method that we describe, it is possible to distinguish between sites of bioactivation of redox active drugs in intact cells.
Mol Pharmacol 1996 Mar
PMID:N-[5-nitro-2-furfurylidene]-3-amino-2-oxazolidinone activation by the human intestinal cell line Caco-2 monitored through noninvasive electron spin resonance spectroscopy. 864 95

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

In the present study, a rat liver cytosolic enzyme responsible for reduction of S-(-)-nicotine-1'-N-oxide to S-(-)-nicotine was investigated. We found that aldehyde oxidase (EC 1.2.3.1) can function as a S-(-)-nicotine-1'-N-oxide reductase in the presence of its electron donor such as 2-hydroxypyrimidine. The apparent K(m) and Vmax values of the enzyme for the N-oxide were 0.24 mM and 30.3 nmol/10 min/mg protein, respectively.
Biochem Mol Biol Int 1996 Oct
PMID:S-(-)-nicotine-1'-N-oxide reductase activity of rat liver aldehyde oxidase. 890 63

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

This study presents data showing individual differences in aldehyde oxidase activity in human and monkey liver cytosols. When assayed with benzaldehyde as a substrate, a significant inter-subject variation in the activity was found in the human liver preparations. When assayed with N1-methylnicotinamide as a substrate, the inter-subject variation of the activity was also observed, but to a lesser extent compared with that of the activity with benzaldehyde. Similarly, variations in aldehyde oxidase activity were found in the monkey liver preparations when assayed with benzaldehyde or N1-methylnicotinamide. The present study suggested that at least two isozymes of aldehyde oxidase exist in the human liver preparations.
Biochem Mol Biol Int 1997 May
PMID:Differences in aldehyde oxidase activity in cytosolic preparations of human and monkey liver. 916 10

The histamine H2-receptor antagonists have been identified as inhibitors of human liver aldehyde dehydrogenase (EC 1.2.1.3) isozymes, E1, E2, and E3. Inhibition was strongest with the E3 isozyme, whose substrates include gamma-aminobutyraldehyde, the aldehyde metabolites of polyamines, and betaine aldehyde. Burimamide, metiamide, cimetidine guanidine, cimetidine, and tiotidine were competitive with aldehyde substrates and noncompetitive with the coenzyme, binding to both the free E3 isozyme and the enzyme-coenzyme binary complex. Cimetidine and tiotidine were the best inhibitors, with Ki values of 1.1 +/- 0.2 microM and 1.0 +/- 0.0 microM, respectively; both are the first ever described potent and selective inhibitors of the E3 isozyme. Examination of the H2-receptor antagonist structures for insight into the moieties accounting for E3 isozyme inhibition pointed to the side-chain polar groups as strongly influencing inhibition, with the cyanoguanidine side chain of cimetidine and tiotidine having the strongest influence. The Ki value of the E3 isozyme for cimetidine was the same as the in vitro dissociation constant for the H2-receptor.
Mol Pharmacol 1997 Aug
PMID:Cimetidine and other H2-receptor antagonists as inhibitors of human E3 aldehyde dehydrogenase. 927 49


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