| Autor: |
Naaz, Huma, Pandey, Veda P., Singh, Swati, Dwivedi, Upendra N. |
| Předmět: |
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| Zdroj: |
Biotechnology & Applied Biochemistry; Mar2013, Vol. 60 Issue 2, p170-189, 20p |
| Abstrakt: |
Ten protein sequences, each of caffeic acid- O-methyltransferase ( COMT) and caffeoyl-coenzyme A- O-methyltransferase ( CCo AOMT), catalyzing methylation of precursors of monolignol from selected dicots and monocots have been analyzed and compared on the basis of their amino acid sequence, motifs/domains, three-dimensional (3 D) structure, and substrate binding. The isoelectric points of all the COMT and CCo AOMT sequences analyzed were found to vary in the p H range of 5 to 6. Molecular weight analyses suggested CCo AOMT to be smaller monomeric proteins (27-29 kDa) as compared with those of COMTs (39-40 kDa), which were dimeric. On the basis of phylogenetic analysis, COMT and CCo AOMT were clustered into two major groups, each of which could be further divided into two subgroups of monocots and dicots. Modeling and superimposition of COMT and CCo AOMT sequences of alfalfa ( Medicago sativa) revealed that both were quite different at the 3 D levels, although they had similarity in the core region. Molecular docking of 16 putative substrates (intermediates of monolignol biosynthesis pathway) revealed that both enzymes interact with all 16 substrates in a similar manner, with thiol esters being the most potent and binding of these putative substrates to CCo AOMT being more efficient. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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