Topic
Aldehyde dehydrogenase
About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.
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TL;DR: It is suggested to measure ALDH activity as a surrogate marker for HSC activity, and to transport and store PBSC under controlled cooling conditions.
Abstract: Aldehyde dehydrogenase activity as a marker for the quality of hematopoietic stem cell transplants
51 citations
TL;DR: In this paper, the authors provide a synopsis of a common structure-function relationship to bridge the gap between the highly studied human ALDHs and lesser so prokaryotic models.
Abstract: Aldehyde dehydrogenases engage in many cellular functions, however their dysfunction resulting in accumulation of their substrates can be cytotoxic. ALDHs are responsible for the NAD(P)-dependent oxidation of aldehydes to carboxylic acids, participating in detoxification, biosynthesis, antioxidant and regulatory functions. Severe diseases, including alcohol intolerance, cancer, cardiovascular and neurological diseases, were linked to dysfunctional ALDH enzymes, relating back to key enzyme structure. An in-depth understanding of the ALDH structure-function relationship and mechanism of action is key to the understanding of associated diseases. Principal structural features 1) cofactor binding domain, 2) active site and 3) oligomerization mechanism proved critical in maintaining ALDH normal activity. Emerging research based on the combination of structural, functional and biophysical studies of bacterial and eukaryotic ALDHs contributed to the appreciation of diversity within the superfamily. Herewith, we discuss these studies and provide our interpretation for a global understanding of ALDH structure and its purpose-including correct function and role in disease. Our analysis provides a synopsis of a common structure-function relationship to bridge the gap between the highly studied human ALDHs and lesser so prokaryotic models.
51 citations
TL;DR: Kinetic analyses support a role for these enzymes in the metabolism of peroxidic aldehydes, which have been reported in ocular tissues, as well as contributing directly to ultraviolet B (UV-B) photoreception.
Abstract: Human aldehyde dehydrogenase isozymes (ALDHs; EC 1.2.1.3) exhibit very high levels of activity in anterior eye tissues. Human corneal ALDH1 and ALDH3 isozymes are present as major soluble proteins (3% and 5%, respectively, of corneal soluble protein) and may play major roles in protecting the cornea against ultraviolet radiation (UVR)-induced tissue damage, as well as contributing directly to ultraviolet B (UV-B) photoreception. The human lens exhibits high levels of ALDH1 activity (1-2% of lens-soluble protein) and lower levels of ALDH3 activity. Kinetic analyses support a role for these enzymes in the metabolism of peroxidic aldehydes, which have been reported in ocular tissues.
50 citations
TL;DR: NAD-dependent succinic semialdehyde dehydrogenase (EC 1.2.1.24) has been purified to homogeneity from human brain via ion-exchange chromatography and affinity chromatography employing BlueSepharose and 5'-AMP Sepharose, which allows the determination of its molecular weight, subunit molecular weight), subunit composition, isoelectric points, and substrate specificity for the first time.
50 citations
TL;DR: A new ALDH, PuuC, from Klebsiella pneumoniae DSM 2026, is reported that efficiently converts 3-HPA to 3-HP and belongs to class 2 ALDHs.
Abstract: 3-Hydroxypropionic acid (3-HP), a versatile and valuable platform chemical, has diverse industrial applications; but its biological production from glycerol is often limited by the capability of the enzyme aldehyde dehydrogenase (ALDH) to convert an intermediary compound, 3-hydroxypropionaldehyde (3-HPA), to 3-HP. In this study, we report a new ALDH, PuuC, from Klebsiella pneumoniae DSM 2026, that efficiently converts 3-HPA to 3-HP. The identified gene puuC was cloned, expressed in Escherichia coli, purified, and characterized for its properties. The recombinant enzyme with a molecular weight of 53.8 kDa exhibited broad substrate specificity for various aliphatic aldehydes, especially C2–C5 aldehydes. NAD+ was the preferred coenzyme for the oxidation of most aliphatic and aromatic aldehydes tested. The optimum pH and temperature for PuuC activity were pH 8.0 and 45°C. The K
m values for 3-HPA and NAD+ were 0.48 and 0.09 mM, respectively. The activity of PuuC was enhanced in the presence of reducing agents such as 2-mercaptoethanol or dithiothreitol, while several metal ions, particularly Hg2+, Ag+, and Cu2+ inhibited its activity. The predicted structure of PuuC indicated the presence of K191 and E194 in close proximity to the glycine motif, suggesting that PuuC belongs to class 2 ALDHs.
50 citations