1b5o

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[[Image:1b5o.jpg|left|200px]]
[[Image:1b5o.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1b5o |SIZE=350|CAPTION= <scene name='initialview01'>1b5o</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1b5o", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1b5o| PDB=1b5o | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5o OCA], [http://www.ebi.ac.uk/pdbsum/1b5o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5o RCSB]</span>
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}}
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'''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1'''
'''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1'''
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[[Category: Nakai, T.]]
[[Category: Nakai, T.]]
[[Category: Ura, H.]]
[[Category: Ura, H.]]
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[[Category: aminotransferase]]
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[[Category: Aminotransferase]]
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[[Category: pyridoxal enzyme]]
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[[Category: Pyridoxal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:06:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:17 2008''
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Revision as of 08:06, 2 May 2008

Image:1b5o.jpg

Template:STRUCTURE 1b5o

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE 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

1B5O is a Single protein structure of sequence from Thermus thermophilus. 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 Page seeded by OCA on Fri May 2 11:06:02 2008

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