Majumder, Arun Lahiri ; Chatterjee, Anirban ; Ghosh Dastidar, Krishnarup ; Majee, Manoj (2003) Diversification and evolution ofL-myo-inositol 1-phosphate synthase1 FEBS Letters, 553 (1-2). pp. 3-10. ISSN 0014-5793
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Official URL: http://doi.org/10.1016/S0014-5793(03)00974-8
Related URL: http://dx.doi.org/10.1016/S0014-5793(03)00974-8
Abstract
L-myo-Inositol 1-phosphate synthase (MIPS, EC 5.5.1.4), the key enzyme in the inositol and phosphoinositide biosynthetic pathway, is present throughout evolutionarily diverse organisms and is considered an ancient protein/gene. Analysis by multiple sequence alignment, phylogenetic tree generation and comparison of newly determined crystal structures provides new insight into the origin and evolutionary relationships among the various MIPS proteins/genes. The evolution of the MIPS protein/gene among the prokaryotes seems more diverse and complex than amongst the eukaryotes. However, conservation of a 'core catalytic structure' among the MIPS proteins implies an essential function of the enzyme in cellular metabolism throughout the biological kingdom.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier B.V. |
| Keywords: | Core structure; L-myo-Inositol 1-phosphate synthase; NAD binding; Oxidoreductase |
| ID Code: | 127839 |
| Deposited On: | 14 Oct 2022 11:43 |
| Last Modified: | 14 Oct 2022 11:43 |
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