Characteristics of alcohol/polyol dehydrogenases

Jörnvall, Hans; Persson, Bengt; Jeffery, Jonathan

doi:10.1111/j.1432-1033.1987.tb13323.x

Cited by 282 publications

(184 citation statements)

References 49 publications

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“…The deduced C. neoformans MPD sequence also contained the conserved Cys residues at positions 55 and 136 and the conserved His residue at position 78, which together form the active site for the zinc ligand. The deduced MPD sequence also contained Cys residues at positions 110, 113, 116 and 124, which are similar to the conserved Cys residues in the second zinc-binding site in yeast alcohol dehydrogenase (Jornvall et al, 1987). Comparison of C. neoformans MPD with other alcohol dehydrogenases also revealed a tetrameric quaternary structure similar to yeast alcohol dehydrogenases, which agrees with the experimental data.…”

Section: Discussionsupporting

confidence: 80%

“…However, a  search of the GenBank and SWISS-PROT databases (Altschul et al, 1997) revealed that the deduced peptide was 43-47 % identical to long-chain alcohol\ polyol dehydrogenases from several fungi and that it was most similar to alcohol dehydrogenase III from Aspergillus nidulans. The deduced peptide also contained conserved residues for cofactor binding (Wierenga & Hol, 1983) and conserved residues for two active sites containing zinc (Jornvall et al, 1987) (Fig. 3).…”

Section: Cloning and Analysis Of The Mpd Cdnamentioning

confidence: 99%

See 1 more Smart Citation

Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase The GenBank accession numbers for the nucleotide sequences for the C. neoformans mannitol-1-phosphate dehydrogenase cDNA and gene are AF175685 and AF186474, respectively.

2000

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Cryptococcus neoformans, the causative agent of cryptococcosis, produces large amounts of mannitol in culture and in infected mammalian hosts. Although there is considerable indirect evidence that mannitol synthesis may be required for wild-type stress tolerance and virulence in C. neoformans, this hypothesis has not been tested directly. It has been proposed that mannitol-1-phosphate dehydrogenase (MPD) is required for fungal mannitol synthesis, but no MPD-deficient fungal mutants or cDNAs or genes encoding fungal MPDs have been described. Therefore, C. neoformans was purified from a 148 kDa homotetramer of 36 kDa subunits that catalysed the reaction mannitol 1-phosphate MNAD ZY fructose 6-phosphate MNADH. Partial peptide sequences were used to isolate the corresponding cDNA and gene, and the deduced MPD protein was found to be homologous to the zinc-containing long-chain alcohol/polyol dehydrogenases. Lysates of Saccharomyces cerevisiae transformed with the cDNA of interest (but not vector-transformed controls) contained MPD catalytic activity. Lastly, Northern analyses demonstrated MPD mRNA in glucose-and mannitol-grown C. neoformans cells. Thus, MPD has been purified and characterized from C. neoformans, and the corresponding cDNA and gene (MPD1) cloned and sequenced. Availability of C. neoformans MPD1 should permit direct testing of the hypotheses that (i) MPD is required for mannitol biosynthesis and (ii) the ability to synthesize mannitol is essential for wild-type stress tolerance and virulence.

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Section: Discussionsupporting

confidence: 80%

Section: Cloning and Analysis Of The Mpd Cdnamentioning

confidence: 99%

Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase The GenBank accession numbers for the nucleotide sequences for the C. neoformans mannitol-1-phosphate dehydrogenase cDNA and gene are AF175685 and AF186474, respectively.

2000

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“…Shortly thereafter, S. cerevisiae ADH4 [78] and E. coli propanediol oxidoreductase [6] were noted to share a significant degree of amino acid identity with Z. mobilis ADH2. Although this new type of ADH lacked homology with any other previously known ADHs [29], they were demonstrated to utilize ethanol, as well as number of other alcohols, as substrate(s) [6]. In the intervening years, a number of additional microbial enzymes of this iron-activated enzyme type have been described [11,32,50,54,73,83].…”

Section: Introductionmentioning

confidence: 94%

“…ADHFE1 also lacks the second of the three conserved histidine residues at the iron-binding region [12]. For the microbial ironactivated ADHs it is these three histidine residues that are thought to be involved in metal binding [29]. These features indicate that human ADHFE1 and its homologs in other species, despite their similarity to iron-activated microbial ADHs, may be of a unique nature in regard to possible enzymatic activities, catalytic mechanism, expression pattern, and function.…”

Section: Introductionmentioning

confidence: 99%

Differentiation-dependent expression of Adhfe1 in adipogenesis

Kim¹,

Tillison²,

Zhou³

et al. 2007

Archives of Biochemistry and Biophysics

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We have determined that adipocytes are a major site of expression of the transcript for the novel alcohol dehydrogenase (ADH), Adhfe1. Adhfe1 is unique in that the sequence of its encoded protein places it among the iron-activated ADHs. Western blot analysis reveals Adhfe1 encodes a 50 kDa cytoplasmic protein and immunocytochemical staining indicates mitochondrial localization. Adhfe1 transcript exhibits differentiation-dependent expression during in vitro brown and white adipogenesis. Unlike many adipocyte-enriched genes, however, Adhfe1 transcript expression in adipocytes is refractory to TNFα-mediated downregulation. However, use of pharmacological inhibitors reveals PI 3-kinase-mediated signals maintain the basal level of Adhfe1 transcript in 3T3-L1 adipocytes. Tissue profiling studies show Adhfe1 transcript is restricted to white and brown adipose tissues, liver, and kidney. In comparison to C57BL/6 mice, Adhfe1 transcript is downregulated 40% in white adipose tissue of ob/ob obese mice. Further characterization of Adhfe1 should yield new insights into adipocyte function and energy metabolism.

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“…Comparison with other ADHs allowed classification of this enzyme into the zinc-containing, medium-chain alcohol/polyol dehydrogenase family which had been primarily described in eukaryotes [5]. Currently, this family is composed of the tetrameric and the dimeric subfamilies which in turn is divided into classes I±VI, C and P [6,7].…”

mentioning

confidence: 99%

Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase

Wilkin¹,

Soetaert²,

Stélandre³

et al. 1999

European Journal of Biochemistry

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A previous study of the effect of zinc deprivation on Mycobacterium bovis BCG pointed out the potential importance of an alcohol dehydrogenase for maintaining the hydrophobic character of the cell envelope. In this report, the effect of the overexpression of the M. bovis BCG alcohol dehydrogenase (ADH) in Mycobacterium smegmatis and M. bovis BCG is described. The purification of the enzyme was performed to apparent homogeneity from overexpressing M. bovis BCG cells and its kinetic parameters were determined. The enzyme showed a strong preference for both aromatic and aliphatic aldehydes while the corresponding alcohols were processed 100±1000-fold less efficiently. The best k cat /K m values were found with benzaldehyde . 3-methoxybenzaldehyde . octanal . coniferaldehyde. A phylogenetic analysis clearly revealed that the M. bovis BCG ADH together with the ADHs from Bacillus subtilis and Helicobacter pylori formed a sister group of the class C medium-chain alcohol dehydrogenases, the plant cinnamyl alcohol dehydrogenases (CADs). Comparison of the kinetic properties of our ADH with some related class C enzymes indicated that the mycobacterial enzyme substrate profile resembled that of the CADs involved in plant defence rather than those implicated in lignification. A possible role for the M. bovis BCG ADH in the biosynthesis of the lipids composing the mycobacterial cell envelope is proposed.Keywords: Mycobacterium bovis BCG; alcohol dehydrogenase; cinnamyl alcohol dehydrogenase.Alcohol dehydrogenases (ADHs) display a wide range of substrate specificities and fulfil several key physiological functions. They can be divided into three major categories. The first category is composed of the NAD(P)-dependent ADHs subdivided into three subgroups according to their metal dependence: (a) the medium-chain zinc-dependent enzymes; (b) the short-chain zinc-independent enzymes; and (c) the iron-activated enzymes. The NAD(P)-independent enzymes form the second category and the third category contains the oxidases which catalyse an essentially irreversible oxidation of alcohols [1].The vaccine strain Mycobacterium bovis BCG grows poorly on zinc-deprived Sauton medium, and forms a thin, pale, unfolded pellicle that gets wet and often sinks. This phenotype suggested a cell envelope with a reduced hydrophobic content. The cell composition and the products excreted into the medium, including aldehydes, can, to some extent, be correlated with a decrease of the specific activity of a soluble zinc-dependent alcohol dehydrogenase. This enzyme was partially purified from BCG cells and characterized as a dimeric NADP-dependent protein of broad specificity with higher affinities towards aldehydes than towards alcohols [2,3].The corresponding gene has been cloned and sequenced [4]. Comparison with other ADHs allowed classification of this enzyme into the zinc-containing, medium-chain alcohol/polyol dehydrogenase family which had been primarily described in eukaryotes [5]. Currently, this family is composed of the tetrameric and the dimeric...

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Characteristics of alcohol/polyol dehydrogenases

Cited by 282 publications

References 49 publications

Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase The GenBank accession numbers for the nucleotide sequences for the C. neoformans mannitol-1-phosphate dehydrogenase cDNA and gene are AF175685 and AF186474, respectively.

Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase The GenBank accession numbers for the nucleotide sequences for the C. neoformans mannitol-1-phosphate dehydrogenase cDNA and gene are AF175685 and AF186474, respectively.

Differentiation-dependent expression of Adhfe1 in adipogenesis

Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase

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