Nonethanol Substrates of Alcohol Dehydrogenase

Pietruszko, Regina

doi:10.1007/978-1-4684-8577-6_6

Cited by 35 publications

(12 citation statements)

References 129 publications

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“…This part of the adrenal gland is responsible for the synthesis of several steroid compounds and hormones. ADH-A2 may be involved in these pathways, since some steroids and fatty acids are known to be ADH-A2 substrates (Pietruszko, 1979).…”

Section: Discussionmentioning

confidence: 99%

Stage and tissue‐specific expression of the alcohol dehydrogenase 1 (Adh‐1) gene during mouse development

Vonesch

Nakshatri

Philippe

et al. 1994

Developmental Dynamics

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The Adh-1 gene product, ADH-A2, the only known murine class I alcohol dehydrogenase, is able to oxidize retinol (vitamin A) into retinaldehyde, the first enzymatic step in the conversion of retinol into its biologically active metabolite retinoic acid. We have investigated the developmental expression pattern of Adh-1 transcripts by in situ hybridization. Transcripts were first detected by embryonic day 10.5 in the mesonephros mesenchyme. During the following gestational days, Adh-1 transcripts were detected in several mesenchymal areas, such as nasal, laterocervical, and genital regions. Adh-1 transcripts were also detected in a small ectodermal domain at the anterior margins of both forelimbs and hindlimbs. During late fetal development, Adh-1 transcripts were found essentially in the epidermis and in a number of tissues which continue to express the gene after birth, such as liver, kidney, gut epithelium, adrenal cortex, testis interstitium, and ovarian stroma. In contrast, a strong expression of Adh-1 was found in the mesenchyme of developing lungs, but not in the adult organ. This highly regulated expression of Adh-1 is discussed with respect to the local synthesis of retinoic acid during development. Although the promoter of the human counterpart of Adh-1 contains a retinoic acid response element (Duester et al. 119913 Mol. Cell. Biol. 11:1638-1646), we report that this element is not conserved in the murine gene. Consistently, Adh-1 promoter-containing reporter constructs were not retinoic acid-inducible in cotransfections assays with RARs and/or RXRs, suggesting that retinoic acid regulation of Adh-1 differs from that of the human gene.

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Section: Discussionmentioning

confidence: 99%

Stage and tissue‐specific expression of the alcohol dehydrogenase 1 (Adh‐1) gene during mouse development

Vonesch

Nakshatri

Philippe

et al. 1994

Developmental Dynamics

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“…Indeed, some MDRs fulfil all these requirements (e.g. broad ADH subfamily [133,136,137], or animal ADH subfamily [15,138]).…”

Section: Is There a Mdr Ancestral Activity?mentioning

confidence: 99%

Diversity, taxonomy and evolution of medium‐chain dehydrogenase/reductase superfamily

Riveros‐Rosas

Julián‐Sánchez

Villalobos‐Molina

et al. 2003

European Journal of Biochemistry

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A comprehensive, structural and functional, in silico analysis of the medium-chain dehydrogenase/reductase (MDR) superfamily, including 583 proteins, was carried out by use of extensive database mining and the BLASTP program in an iterative manner to identify all known members of the superfamily. Based on phylogenetic, sequence, and functional similarities, the protein members of the MDR superfamily were classified into three different taxonomic categories: (a) subfamilies, consisting of a closed group containing a set of ideally orthologous proteins that perform the same function; (b) families, each comprising a cluster of monophyletic subfamilies that possess significant sequence identity among them and might share or not common substrates or mechanisms of reaction; and (c) macrofamilies, each comprising a cluster of monophyletic protein families with protein members from the three domains of life, which includes at least one subfamily member that displays activity related to a very ancient metabolic pathway. In this context, a superfamily is a group of homologous protein families (and/or macrofamilies) with monophyletic origin that shares at least a barely detectable sequence similarity, but showing the same 3D fold.The MDR superfamily encloses three macrofamilies, with eight families and 49 subfamilies. These subfamilies exhibit great functional diversity including noncatalytic members with different subcellular, phylogenetic, and species distributions. This results from constant enzymogenesis and proteinogenesis within each kingdom, and highlights the huge plasticity that MDR superfamily members possess. Thus, through evolution a great number of taxa-specific new functions were acquired by MDRs. The generation of new functions fulfilled by proteins, can be considered as the essence of protein evolution. The mechanisms of protein evolution inside MDR are not constrained to conserve substrate specificity and/or chemistry of catalysis. In consequence, MDR functional diversity is more complex than sequence diversity.MDR is a very ancient protein superfamily that existed in the last universal common ancestor. It had at least two (and probably three) different ancestral activities related to formaldehyde metabolism and alcoholic fermentation. Eukaryotic members of this superfamily are more related to bacterial than to archaeal members; horizontal gene transfer among the domains of life appears to be a rare event in modern organisms.Keywords: protein taxonomy; protein evolution; mediumchain alcohol dehydrogenase; enoyl reductase; formaldehyde dehydrogenase.Correspondence to H. Riveros-Rosas, Depto. Bioquı´mica, Fac. Medicina, UNAM, Apdo. Postal 70-159, Cd. Universitaria, Me´xico, 04510, D.F., Me´xico. Fax: + 52 55 5616 2419, Tel.: + 52 55 5622 0829, E-mail: hriveros@servidor.unam.mx Abbreviations: AADH, allyl alcohol dehydrogenase; ACR, acyl-CoA reductase; ADH, alcohol dehydrogenase; AL, alginate lyase; ARP, auxinregulated protein; AST, membrane traffic protein; BCHC, 2-desacetyl-2-hydroxyethyl bacteriochlorophyll...

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“…Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) possess a high affinity for ethanol and catalyse the oxidation or reduction of a wide spectrum of substrates [1]. Human ADH exists in multiple molecular forms grouped into several classes.…”

Section: Introductionmentioning

confidence: 99%

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in breast cancer

et al. 2006

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Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) play a significant role in the metabolism of many biological substances. ADH participates in the metabolism of ethanol, retinoic acid, lipid peroxidation products, leukotriene and glutathione metabolism. ALDH is responsible for oxidation of acetaldehyde and other aldehydes and metabolism of histamine and retinoic acid. The aim of this study was to compare the metabolism in breast cancer cells and normal breast parenchyma by measuring ADH isoenzymes and ALDH activities in these tissues. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline (NDMA) as a substrate. For the measurement of the activity of ALDH and class I and II isoenzymes of ADH we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was detected by the photometric method with n-octanol and class IV with m-nitrobenzaldehyde as substrates. The samples were taken surgically during resection of breast carcinoma from 75 women. The activity of the class I ADH isoenzyme was significantly lower in breast cancer cells than in healthy tissues. The other tested classes of ADH had a tendency for higher levels of activity in cancer cells than in normal mammary tissue. The activity of total ADH and ALDH was also not significantly lower in the cancer cells. The decrease of activity of class I ADH isoenzyme in breast cancer tissues may be a factor of some disorders in metabolic pathways with participation of these isoenzymes that can lead to carcinogenesis.

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Nonethanol Substrates of Alcohol Dehydrogenase

Cited by 35 publications

References 129 publications

Stage and tissue‐specific expression of the alcohol dehydrogenase 1 (Adh‐1) gene during mouse development

Stage and tissue‐specific expression of the alcohol dehydrogenase 1 (Adh‐1) gene during mouse development

Diversity, taxonomy and evolution of medium‐chain dehydrogenase/reductase superfamily

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in breast cancer

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