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| {{STRUCTURE_5bj3| PDB=5bj3 | SCENE= }} | | {{STRUCTURE_5bj3| PDB=5bj3 | SCENE= }} |
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| '''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1'''
| | ===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1=== |
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| ==Overview==
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| Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11432784}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Aminotransferase]] | | [[Category: Aminotransferase]] |
| [[Category: Pyridoxal enzyme]] | | [[Category: Pyridoxal enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:32:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:57:00 2008'' |