Ramasarma, T (1994) One protein�many functions. In: Current Science (Bangalore), 67 (1). 24-29 .
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Abstract
The concept of one enzyme-one activity had influenced biochemistry for over half a century. Over 1000 enzymes are now described. Many of them are highly 'specific'. Some of them are crystallized and their three-dimensional structures determined. They range from 12 to 1000 kDa in molecular weight and possess 124 to several hundreds of amino acids. They occur as single polypeptides or multiple-subunit proteins. The active sites are assembled on these by appropriate tertiary folding of the polypeptide chain, or by interaction of the constituent subunits. The substrate is held by the side-chains of a few amino acids at the active site on the surface, occupying a tiny fraction of the total area. What is the bulk of the protein behind the active site doing? Do all proteins have only one function each? Why not a protein have more than one active site on its large surface? Will we discover more than one activity for some proteins? These newer possibilities are emerging and are finding experimental support. Some proteins purified to homogeneity using assay methods for different activities are now recognized to have the same molecular weight and a high degree of homology of amino acid sequence. Obviously they are identical. They represent the phenomenon of one protein-many functions.
Item Type: | Journal Article |
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Publication: | Current Science (Bangalore) |
Publisher: | Indian Academy of Sciences |
Additional Information: | Copyright of this article belongs to Indian Academy of Sciences. |
Department/Centre: | Division of Biological Sciences > Biochemistry |
Date Deposited: | 20 May 2011 09:47 |
Last Modified: | 20 May 2011 09:47 |
URI: | http://eprints.iisc.ac.in/id/eprint/36661 |
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