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amino acod

Zhu Shiyun, Zheng Xuesong, Li Daotang
Ozonation of 11 naphthalene sulfonic acids (NSA) in the aqueous solution was studied by bubbling at 31 degrees C at an ozone dose rate of 5.56 mg min(-1) l(-1). COD, TOC and BOD5 of these compounds were tested. It was found that COD and TOC can be removed effectively by ozonation as expected. More than 40% COD of compounds No. I (2-amino-1-NSA), No. 5 (1-hydroxy-7-amino-5-NSA), No. 6 (6-hydroxy-1-NSA), No. 8 (6-amino-1,4-naphthalene disulfonic acid) and No. 11 (I -hydroxy-6-amino-3-NSA) has been eliminated at an ozone dosage of 5...
March 2002: Water Research
H Bergeron, D Labbé, C Turmel, P C Lau
The degradation of 1,2-dichloroethane (DCE) by Xanthobacter autotrophicus GJ10 proceeds via chloroacetaldehyde (CAA), a toxic intermediate in the cells if it is not metabolized further by the NAD(+)-dependent CAA dehydrogenases. Here, we describe the cloning, sequence and expression in Escherichia coli of aldA, a plasmid-located CAA dehydrogenase-encoding gene of GJ10 as well as a chromosomal homolog, designated aldB. The DNA-predicted amino acid (aa) sequences of the two proteins (505 aa in AldA and 506 aa in AldB) are 84% identical...
January 19, 1998: Gene
H L Peng, W L Deng, Y H Yang, H Y Chang
The acoD gene, which encodes a dihydrolipoamide dehydrogenase component of the acetoin dehydrogenase enzyme system of Klebsiella pneumoniae was isolated and the nucleotide sequence determined. The gene is capable of encoding a protein of 465 amino acid residues with conserved binding domains for NAD and FAD, and two redox-active cysteine residues. The acoD gene product exhibited a Michaelis constant of 170 microM for NAD, while NADP can not be used as a substrate. The purified enzyme appeared to be a dimer of the acoD gene product...
June 1996: Journal of Biochemistry
J Xu, R C Johnson
Escherichia coli aldB was identified as a gene that is negatively regulated by Fis but positively regulated by RpoS. The complete DNA sequence determined in this study indicates that aldB encodes a 56.3-kDa protein which shares a high degree of homology with an acetaldehyde dehydrogenase encoded by acoD of Alcaligenes eutrophus and an aldehyde dehydrogenase encoded by aldA of Vibrio cholerae and significant homology with a group of other aldehyde dehydrogenases from prokaryotes and eukaryotes. Expression of aldB is maximally induced during the transition from exponential phase to stationary phase...
June 1995: Journal of Bacteriology
A J Clark, C Y Umezawa, M E Swendseid
No abstract text is available yet for this article.
November 1973: American Journal of Clinical Nutrition
H Priefert, N Krüger, D Jendrossek, B Schmidt, A Steinbüchel
The N-terminal amino acid sequence of purified acetaldehyde dehydrogenase II (AcDH-II) from ethanol-grown cells of Alcaligenes eutrophus was determined. By using oligonucleotides deduced from this sequence the structural gene for AcDH-II, which was referred to as acoD, was localized on a 7.2-kbp EcoRI restriction fragment (fragment D), which has been cloned recently (C. Fründ, H. Priefert, A. Steinbüchel, and H. G. Schlegel, J. Bacteriol. 171:6539-6548, 1989). A 2.8-kbp PstI subfragment of D, which harbored acoD, was sequenced...
February 1992: Journal of Bacteriology
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