5bj3: Difference between revisions
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|PDB= 5bj3 |SIZE=350|CAPTION= <scene name='initialview01'>5bj3</scene>, resolution 2.2Å | |PDB= 5bj3 |SIZE=350|CAPTION= <scene name='initialview01'>5bj3</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5 | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | ||
|GENE= | |GENE= | ||
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[[Category: pyridoxal enzyme]] | [[Category: pyridoxal enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 16:05:12 2008'' | ||
Revision as of 14:05, 23 March 2008
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| 5bj3, resolution 2.2Å | |||||||||||||
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| Ligands: | PLP | ||||||||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1
Overview
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.
About this Structure
5BJ3 is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
Substrate recognition mechanism of thermophilic dual-substrate enzyme., Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S, J Biochem. 2001 Jul;130(1):89-98. PMID:11432784
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