scholarly journals An Alcohol Dehydrogenase 3 (ADH3) from Entamoeba histolytica Is Involved in the Detoxification of Toxic Aldehydes

2020 ◽  
Vol 8 (10) ◽  
pp. 1608
Author(s):  
Constantin König ◽  
Martin Meyer ◽  
Corinna Lender ◽  
Sarah Nehls ◽  
Tina Wallaschkowski ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Entamoeba Histolytica ◽  
Biochemical Characterization ◽  
Stop Codon ◽  
In Silico Analysis ◽  
Peptidase Activity ◽  
Stool Samples ◽  
Human Stool

Recently, a putative alcohol dehydrogenase 3, termed EhADH3B of the Entamoeba histolytica isolate HM-1:IMSS was identified, which is expressed at higher levels in non-pathogenic than in pathogenic amoebae and whose overexpression reduces the virulence of pathogenic amoebae. In an in silico analysis performed in this study, we assigned EhADH3B to a four-member ADH3 family, with ehadh3b present as a duplicate (ehadh3ba/ehadh3bb). In long-term laboratory cultures a mutation was identified at position 496 of ehadh3ba, which codes for a stop codon, which was not the case for amoebae isolated from human stool samples. When using transfectants that overexpress or silence ehadh3bb, we found no or little effect on growth, size, erythrophagocytosis, motility, hemolytic or cysteine peptidase activity. Biochemical characterization of the recombinant EhADH3Bb revealed that this protein forms a dimer containing Ni2+ or Zn2+ as a co-factor and that the enzyme converts acetaldehyde and formaldehyde in the presence of NADPH. A catalytic activity based on alcohols as substrates was not detected. Based on the results, we postulate that EhADH3Bb can reduce free acetaldehyde released by hydrolysis from bifunctional acetaldehyde/alcohol dehydrogenase-bound thiohemiacetal and that it is involved in detoxification of toxic aldehydes produced by the host or the gut microbiota.

Electron probe analysis and biochemical characterization of electron-dense granules secreted by Entamoeba histolytica

1997 ◽  
Vol 85 (2) ◽  
pp. 233-242 ◽  
Author(s):  
Gloria León ◽  
Charles Fiori ◽  
Pradeep Das ◽  
Miguel Moreno ◽  
Rosalinda Tovar ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Electron Probe ◽  
Biochemical Characterization ◽  
Electron Probe Analysis ◽  
Dense Granules ◽  
Probe Analysis

Highly sensitive and specific detection of Giardia duodenalis, Entamoeba histolytica, and Cryptosporidium spp. in human stool samples by the BD MAX™ Enteric Parasite Panel

2017 ◽  
Vol 117 (2) ◽  
pp. 447-451 ◽  
Author(s):  
Marijo Parčina ◽  
Ingrid Reiter-Owona ◽  
Frank P. Mockenhaupt ◽  
Valerija Vojvoda ◽  
Jean Bosco Gahutu ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Giardia Duodenalis ◽  
Specific Detection ◽  
Cryptosporidium Spp ◽  
Highly Sensitive ◽  
Stool Samples ◽  
Human Stool

scholarly journals Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosu s

2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Biochemical Characterization ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Short Chain Alcohol

scholarly journals Biochemical Characterization of Phenylacetaldehyde Dehydrogenases from Styrene-degrading Soil Bacteria

2020 ◽  
Author(s):  
Juliane Zimmerling ◽  
Michel Oelschlägel ◽  
Carolin Großmann ◽  
Matthias Voitel ◽  
Michael Schlömann ◽  
...  
Keyword(s):  
Esterase Activity ◽  
Soil Bacteria ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Aldehyde Dehydrogenases ◽  
Long Term Stability ◽  
Almost All ◽  
Different Characteristics

Abstract Four phenylacetaldehyde dehydrogenases (designated as FeaB or StyD) originating from styrene-degrading soil bacteria were biochemically investigated. In this study, we focused on the Michaelis-Menten kinetics towards the presumed native substrate phenylacetaldehyde and the obviously preferred co-substrate NAD+. Furthermore, the substrate specificity on four substituted phenylacetaldehydes and the co-substrate preference were studied. Moreover, these enzymes were characterized with respect to their temperature as well as long-term stability. Since aldehyde dehydrogenases are known to show often dehydrogenase as well as esterase activity, we tested this capacity, too. Almost all results showed clearly different characteristics between the FeaB and StyD enzymes. Furthermore, FeaB from Sphingopyxis fribergensis Kp5.2 turned out to be the most active enzyme with an apparent specific activity of 17.8 ± 2.1 U mg-1. Compared with that, both StyDs showed only activities less than 0.2 U mg-1 except the overwhelming esterase activity of StyD-CWB2 (1.4 ± 0.1 U mg-1). The clustering of both FeaB and StyD enzymes with respect to their characteristics could also be mirrored in the phylogenetic analysis of twelve dehydrogenases originating from different soil bacteria.

Gene Cloning and Biochemical Characterization of an Alcohol Dehydrogenase fromEuglena gracilis

2008 ◽  
Vol 55 (6) ◽  
pp. 554-561 ◽  
Author(s):  
HELGA N. PALMA-GUTIÉRREZ ◽  
JOSÉ SALUD RODRÍGUEZ-ZAVALA ◽  
RICARDO JASSO-CHÁVEZ ◽  
RAFAEL MORENO-SÁNCHEZ ◽  
EMMA SAAVEDRA
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gene Cloning ◽  
Biochemical Characterization

scholarly journals Bioinformatics structural and phylogenetic characterization of Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2)

BIOS ◽  
2019 ◽  
Vol 90 (1) ◽  
pp. 30
Author(s):  
Katie M. Lowerre ◽  
Avelina Espinosa ◽  
Guillermo Paz-y-Miño-C ◽  
Christopher Hemme
Keyword(s):  
Alcohol Dehydrogenase ◽  
Entamoeba Histolytica ◽  
Phylogenetic Characterization ◽  
Alcohol Dehydrogenase 2

scholarly journals Purification and molecular characterization of the NAD+-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica

1994 ◽  
Vol 303 (3) ◽  
pp. 743-748 ◽  
Author(s):  
I Bruchhaus ◽  
E Tannich
Keyword(s):  
Alcohol Dehydrogenase ◽  
Entamoeba Histolytica ◽  
Dna Sequences ◽  
Microscopic Analysis ◽  
Kinetic Studies ◽  
Protozoan Parasite ◽  
Striking Similarity ◽  
Electron Microscopic ◽  
Catalytic Functions

A bifunctional 95 kDa polypeptide (EhADH2) harbouring acetaldehyde dehydrogenase and alcohol dehydrogenase activities was purified to homogeneity from trophozoite extracts of the protozoan parasite Entamoeba histolytica. Kinetic studies revealed that the enzyme utilizes NAD+ rather than NADP+ as cofactor. Km values for acetyl-CoA, acetaldehyde and ethanol were found to be 0.015, 0.15 and 80 mM respectively in the presence of 0.2 mM NAD+. The primary structure of EhADH2 as deduced from respective amoebic DNA sequences showed striking similarity to the trifunctional AdhE protein of Escherichia coli and the bifunctional AAD protein of Clostridium acetobutylicum. Alignment with a number of aldehyde dehydrogenases and alcohol dehydrogenases from various species suggested that the two catalytic functions of EhADH2 are located on separate parts of the molecule. By cross-linking experiments and electron-microscopic analysis, native EhADH2 was found to be organized in a homopolymeric fashion consisting of more than 20 associated promoters which form rods about 50-120 nm in length.

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