Transketolase : An Essential Component Of Many Enzymatic, Biochemical Processes

Transketolase : An Essential Component Of Many Enzymatic, Biochemical Processes

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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).
To understand the processes a little better, in the carbon-reactions pathway, transketolase functions in the chloroplast stroma – which will be discussed further in the paper. “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,, 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 (U...

... middle of paper ...

... a magnesium- and thiamine-pyrophosphate-binding site; and 73, 113 through 115, 145, 146, 285 and 366 – all of which are one amino acid in length, each, and thiamine-pyrophosphate-binding sites. The actual sequence’s chain begins at 1 and ends at 642 (Ikeda et al, 2003). None of the amino acids are removed.
Transketolase is not just a coenzyme of its own, but it has several families and sub-families. The aforementioned are only a few of the hundreds of species in existence. Most of these families are transferase in functionality – yet with their own subtle differences and locales. However, like all transketolase enzymes, they all have a common cofactor of thiamine pyrophosphate. This is necessary for the catalytic reactions in the carbon-reactions and pentose phosphate pathways.

Encoding Dihydroxyacetone Synthase…,” November 1998: Journal of Bacteriology; 180(22).

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