Abstract - 2qgnA: Difference between revisions
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tRNA isopentenyltransferase (tRNA-IPT) is an important enzyme that catalyses the biosynthesis of cytokinins. Cytokinins are modified adenine which can be present in the tRNA-free or tRNA-bound form. Such modification at specific position of the target tRNA influences its molecular function. This family of enzyme is conserved in all organisms including plants, microorganisms and higher eukaryotes. The structure of this protein is first determined in Bacillus halodurans and the human tRNA-IPT has been recently cloned. The latter is found to have a C2H2 zinc finger motif which is also found in other organisms except prokaryotes. | tRNA isopentenyltransferase (tRNA-IPT) is an important enzyme that catalyses the biosynthesis of cytokinins. | ||
Cytokinins are modified adenine which can be present in the tRNA-free or tRNA-bound form. Such modification at specific position of the target tRNA influences its molecular function. This family of enzyme is conserved in all organisms including plants, microorganisms and higher eukaryotes. The structure of this protein is first determined in Bacillus halodurans and the human tRNA-IPT has been recently cloned. The latter is found to have a C2H2 zinc finger motif which is also found in other organisms except prokaryotes. | |||
Revision as of 13:26, 31 May 2008
tRNA isopentenyltransferase (tRNA-IPT) is an important enzyme that catalyses the biosynthesis of cytokinins.
Cytokinins are modified adenine which can be present in the tRNA-free or tRNA-bound form. Such modification at specific position of the target tRNA influences its molecular function. This family of enzyme is conserved in all organisms including plants, microorganisms and higher eukaryotes. The structure of this protein is first determined in Bacillus halodurans and the human tRNA-IPT has been recently cloned. The latter is found to have a C2H2 zinc finger motif which is also found in other organisms except prokaryotes.
