Wai-Kwan Tang

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Antiquitin is an evolutionarily conserved protein believed to play a role in the regulation of cellular turgor. Based on sequence analysis, this protein is classified as a member of the aldehyde dehydrogenase superfamily. All previous studies on antiquitin have been confined to the nucleotide level, and the protein has never been purified and characterized.(More)
The crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8A resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin's(More)
Subsequent to our earlier report on the first purification of antiquitin protein from seabream liver and demonstration of its enzymatic activity [FEBS Letters 516 (2002) 183-186], we report herein the cloning of its full-length cDNA sequence. The open reading frame encodes a protein of 511 amino acids. Results of RT-PCR indicate that antiquitin is highly(More)
Antiquitin is an aldehyde dehydrogenase involved in the catabolism of lysine. Mutations of antiquitin have been linked with the disease pyridoxine-dependent seizures. While it is well established that lysine metabolism takes place in the mitochondrial matrix, evidence for the mitochondrial localization of antiquitin has been lacking. In the present study,(More)
Wide field-of-view (FOV) is necessary for many industrial applications, such as air traffic control, large vehicle driving and navigation. Unfortunately, the supporting structure/frame in most systems usually blocks part of the view, results in "blind spot" and raises the risk. In some cases, the working site is hazardous to the pilot. In this video(More)
Aldehyde dehydrogenase (ALDH) is a superfamily of enzymes catalyzing the conversion of various aldehydes to the corresponding acids using the coenzymes NAD+ or NADP+. While mammalian ALDHs have been studied extensively, the non-mammalian ALDHs, notably those of teleostean origin, remain relatively unexplored. In our previous study on grass carp(More)
Antiquitin (ALDH7) is a member of the aldehyde dehydrogenase superfamily. In plants, ALDH7 is inducible upon dehydration and is thus believed to possess an osmoregulatory role. On the other hand, however, its exact physiological function in animals remains elusive. We herein report the isolation of the black seabream (Acanthopagrus schlegeli) antiquitin(More)
Two aldehyde dehydrogenases (ALDH) were purified from the liver of black seabream (Acanthopagrus schlegeli). Chromatography of the liver homogenate on an alpha-cyanocinnamate-Sepharose affinity column results in two activity peaks using acetaldehyde as the substrate. The eluate was subjected to another affinity chromatography on(More)
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