Introduction to DHRS1
Short-chain Dehydrogenase/Reductase (SDR) is a large protein family currently numbering about 3000 members (Kallberg et al. 2002b). It also goes by the alternative name of the tyrosine-dependent oxidoreductase protein family because of their conserved tyrosine residue at position 152. (Edgar. 2002)The SDR family is defined by a rossman fold, and highly conserved Ser, Tyr and Lys residues (Kallberg et al 2002a). SDR proteins have a length of about 250 amino acids (aa) and show approximately 15-30% sequence similarity/identity. This is relatively low when compared to other families. (Tramontano, A. 1998). Despite this, members still have large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains (Benyajati et al. 1981).
Dehydrogenase/Reductase member 1 (DHRS1) is one member of the SDR family found in chromosome 14 in Homo sapiens. (Wu Q, et al. 2001) The role of a dehydrogenase is to oxidize substrates, that is the removal of electrons (Refer to Figure 1) (Takahoma, 1983). The acceptor is generally a NAD+/NADP. NAD (Nicotinamide adenine dinucleotide is found in all living cells. The role of NAD+ in cells is to carry electrons from one reaction to another. Reductase enzymes lower activation energy in reduction reactions. Reduction reactions involve the gain of electrons (Fig 1). Activation energy is the amount of energy needed to be overcome in order for a chemical reaction to occur.
Currently the exact function of DHRS1 is unpublished. The objective of this project was to find relative functional, structural and evolutional information on DHRS1 in order to make an appropriate conclusion about its role in organism function.
Abstract | Introduction | Results | Discussion | Conclusion | Method | References
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