Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently.
Aldehyde dehydrogenase 1 family member A2 (ALDH1A2), also known as retinaldehyde dehydrogenase 2 (RALDH2), belongs to the aldehyde dehydrogenase family which contains two members, the ALDH1 s (ALDH1A1, ALDH1A2 and ALDH1A3) and the 9-cis retinaldehyde dehydrogenase ALDH8 s. ALDH1A2 is key enzyme that catalyzes the synthesis of retinoic acid (RA) from retinaldehyde. RA is a paracrine hormone signaling molecule that functions in developing and adult tissues. ALDH1A2 was also found to regulate normal and tumor cell growth and differentiation. Several studies showed that ALDH1A2 expression is increased after the appearance of AraC resistance in clinical cases which means this protein is effective in AraC resistance.
Aldehyde dehydrogenase 1 family member A3 (ALDH1A3), also known as retinaldehyde dehydrogenase 3 (RALDH3), is a member of the aldehyde dehydrogenase family known to metabolize a wide variety of aldehydes. ALDH1A3 specifically oxidizes retinal to retinoic acid (RA) and is differentially expressed in developing embryonic tissues and adult organs. The RA produced by ALDH1A3 in rodents contributes to the development of skin and hair follicles, brain, tooth buds, lungs, olfactory bulbs, kidneys, eyes, skeletal muscle and seminal vesicles. In recent research, ALDH1A3 could be as a marker of cancer stem cell to predict metastasis or clinical prognosis in many cancers.
Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme that catalyzes the oxidation of various aldehydes. Certain types of epithelial tissues in mammals, especially those continually exposed to environmental stress (e.g., corneal epithelium), express ALDH3A1 at high levels and its abundance in such tissues is perceived to help to maintain cellular homeostasis under conditions of oxidative stress. Metabolic as well as non-metabolic roles for ALDH3A1 have been associated with its mediated resistance to cellular oxidative stress. Aldehyde dehydrogenase 1A1 (ALDH1A1) and ALDH3A1 are corneal crystallins. They protect inner ocular tissues from ultraviolet radiation (UVR)-induced oxidative damage through catalytic and non-catalytic mechanisms. Additionally, ALDH3A1 has been postulated to play a regulatory role in the corneal epithelium based on several studies that report an inverse association between ALDH3A1 expression and corneal cell proliferation. ALDH3A1 plays an important role in many cellular oxidative processes, including cancer chemoresistance, by metabolizing activated forms of oxazaphosphorine drugs such as cyclophosphamide (CP) and its analogues. Compounds that can selectively target ALDH3A1 could permit delineation of its roles in these processes and could restore chemosensitivity in cancer cells that express this isoenzyme. ALDH3A1 may act to protect corneal cells against cellular oxidative damage by metabolizing toxic lipid peroxidation products (e.g., 4-HNE), maintaining cellular GSH levels and redox balance, and operating as an antioxidant.
Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene, belongs to the aldehyde dehydrogenase family. ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
ALDH4A1 is a member of the aldehyde dehydrogenase family. Aldehyde dehydrogenase enzymes function in the metabolism of many molecules including certain fats (cholesterol and other fatty acids) and protein building blocks (amino acids). Additional aldehyde dehydrogenase enzymes detoxify external substances, such as alcohol and pollutants, and internal substances, such as toxins that are formed within cells. ALDH4A1 is expressed abundantly in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas. It is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Defects in ALDH4A1 are the cause of hyperprolinemia type 2 (HP-2). HP-2 is characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
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