1gck: Difference between revisions

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[[Image:1gck.jpg|left|200px]]
{{Seed}}
[[Image:1gck.png|left|200px]]


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{{STRUCTURE_1gck|  PDB=1gck  |  SCENE=  }}  
{{STRUCTURE_1gck|  PDB=1gck  |  SCENE=  }}  


'''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE'''
===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE===




==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.
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{{ABSTRACT_PUBMED_11432784}}


==About this Structure==
==About this Structure==
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[[Category: Dual-substrate enzyme]]
[[Category: Dual-substrate enzyme]]
[[Category: Pyridoxal enzyme]]
[[Category: Pyridoxal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:05:00 2008''

Revision as of 02:05, 1 July 2008

File:1gck.png

Template:STRUCTURE 1gck

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE

Template:ABSTRACT PUBMED 11432784

About this Structure

1GCK 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

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