Molybdoprotein aldehyde dehydrogenases from comamonas testosteroni and amycolatopsis methanolica

1995 ◽  
Vol 59 (2-3) ◽  
pp. 741
Author(s):  
D.M.A.M. Luykx ◽  
S.W. Kim ◽  
S. de Vries ◽  
J.A. Duine
1998 ◽  
Vol 37 (4-5) ◽  
pp. 171-175
Author(s):  
Artem Khlebnikov ◽  
Falilou Samb ◽  
Paul Péringer

p-toluenesulphonic acid degradation by Comamonas testosteroni T-2 in multi-species biofilms was studied in a fixed bed biofilm reactor. The polypropylene static mixer elements (Sulzer Chemtech Ltd., Switzerland) were used as a support matrix for biofilm formation. Biofilm respiration was estimated using the dynamic gassing-out oxygen uptake method. A strong relation between oxygen uptake and reactor degradation efficiency was observed, because p-toluenesulphonate degradation is a strictly aerobic process. This technique also allowed us to estimate the thickness of the active layer in the studied system. The mean active thickness was in order of 200 μm, which is close to maximum oxygen penetration depth in biofilms. A transient mathematical model was established to evaluate oxygen diffusitivity in non-steady-state biofilms. Based on the DO concentration profiles, the oxygen diffusion coefficient and the maximum respiration activity were calculated. The oxygen diffusion coefficient obtained (2 10−10-1.2 10−9 m2 s−1) is in good agreement with published values. The DO diffusion coefficient varied with biofilm development. This may be, most likely, due to the biofilm density changes during the experiments. The knowledge of diffusivity changes in biofilms is particularly important for removal capacity estimation and appropriate reactor design.


1987 ◽  
Vol 262 (23) ◽  
pp. 10911-10913
Author(s):  
K H Jones ◽  
R Lindahl ◽  
D C Baker ◽  
R Timkovich

Genes ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 51
Author(s):  
Adesola J. Tola ◽  
Amal Jaballi ◽  
Hugo Germain ◽  
Tagnon D. Missihoun

Abiotic and biotic stresses induce the formation of reactive oxygen species (ROS), which subsequently causes the excessive accumulation of aldehydes in cells. Stress-derived aldehydes are commonly designated as reactive electrophile species (RES) as a result of the presence of an electrophilic α, β-unsaturated carbonyl group. Aldehyde dehydrogenases (ALDHs) are NAD(P)+-dependent enzymes that metabolize a wide range of endogenous and exogenous aliphatic and aromatic aldehyde molecules by oxidizing them to their corresponding carboxylic acids. The ALDH enzymes are found in nearly all organisms, and plants contain fourteen ALDH protein families. In this review, we performed a critical analysis of the research reports over the last decade on plant ALDHs. Newly discovered roles for these enzymes in metabolism, signaling and development have been highlighted and discussed. We concluded with suggestions for future investigations to exploit the potential of these enzymes in biotechnology and to improve our current knowledge about these enzymes in gene signaling and plant development.


1985 ◽  
Vol 45 (6) ◽  
pp. 1903-1910 ◽  
Author(s):  
Jacques-Andre Maring ◽  
Richard A. Deitrich ◽  
Roger Little

1977 ◽  
Vol 164 (1) ◽  
pp. 119-123 ◽  
Author(s):  
Ronald Lindahl

The pre- and post-natal ontogeny of Sprague–Dawley rat liver aldehyde dehydrogenase [aldehyde–NAD(P)+ oxidoreductase, EC 1.2.1.5] is described. At no time in its ontogenetic development does normal liver aldehyde dehydrogenase exhibit any of the characteristics of a series of unique aldehyde dehydrogenases that can be isolated from 2-acetamidofluorene-induced rat hepatomas. Enzyme activity is first detectable in 15-day foetal liver and gradually increases throughout pre- and post-natal development until adult activities are attained by day 49 after birth. Electrophoretically, normal aldehyde dehydrogenase, throughout its ontogeny, exists as the same single isoenzyme found in normal adult liver. Isoelectric points for two normal liver isoenzymes demonstrable by isoelectric focusing are pH5.9 and 6.0. The immunochemical properties of aldehyde dehydrogenase during its ontogeny are identical with those of normal adult liver aldehyde dehydrogenase when tested against anti-(hepatoma aldehyde dehydrogenase) serum in Ouchterlony double-diffusion tests. The results indicate that the hepatoma-specific aldehyde dehydrogenases are not the result of the de-repression of genes normally repressed in adult rat liver or in some other adult tissue.


Nitric Oxide ◽  
2008 ◽  
Vol 19 ◽  
pp. 32-33
Author(s):  
Matteo Beretta ◽  
Michael Russwurm ◽  
Doris Koesling ◽  
Kurt Schmidt ◽  
Bernd Mayer

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