Importance Of Transketolase

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Transketolase is an essential component of many enzymatic, biochemical processes. According to the National Center of Biotechnology Information, in conjunction with a self-paraphrased definition, transketolase is a thiamine pyrophosphate, metabolic coenzyme which is partly responsible for various catalytic reactions, sucrose breakdowns and chemical, ketose transports. Albert L. Lehninger, Michael Cox and David R. Nelson, the authors of Lehninger Principles of Biochemistry, confirm this proposed definition in the works of their book (2005). Transketolase functions in two general areas of interest: the carbon-reactions pathway (in plants, formerly referred to as the “Calvin cycle”) and the pentose phosphate pathway (in, both, plants and animals). …show more content…

“Transketolase,” as is, is just a general form of the word – almost a standard. There are several families and sub-families. To give a standard of transketolase’s presence in humans, let us look at specifics. Transketolase (TK or TKT) is assigned the number, 2.2.1.1., by the Enzyme Commission (EC). As a part but not limited to, it functions in homo-sapiens or humans (though there are species which only function in plant life as well). Transketolase has a complete protein sequence length of 623 AA. Within the cell, specifically, TK is located in the nucleus and cytosol. Understanding transketolase’s function is quintessential. Its function is the “catalyzation of the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (Universal Protein Resource, Transketolase, 2002-2014).” The total length of the protein chain goes from amino acid #1 to #623. However, one of the more important regions is from 123 through 125, where nucleotide binding occurs. This region is three amino acids in length and is comprised of thiamine pyrophosphate. Also, the proton donor is #366 in the protein sequence. Transketolase is more detail than is commonly …show more content…

Some important AA sites within the protein sequence are: 431 – which is one amino acid in length, a proton donor and a binding site for thiamine pyrophosphate; 167 – which is one amino acid in length and a metal binding site; 197 – which is one amino acid in length and a binding site for, both, magnesium and thiamine pyrophosphate; 76 and 459 – which are, both, one amino acid in length and binding sites for thiamine pyrophosphate; 273 – which is one amino acid in length, a binding site for thiamine pyrophosphate and an essential site for catalytic activity; and 126 through 128 – which, altogether, comprise three amino acids in length and are the sites for nucleotide binding of thiamine pyrophosphate. The actual sequence’s chain begins at 2 and ends at 706 (Sakai et al, 1998); the first in the sequence (“1”) is removed as the methionine initiator. However, the “family tree”

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