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1b5o

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[[Image:1b5o.jpg|left|200px]]
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{{Seed}}
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[[Image:1b5o.png|left|200px]]
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{{STRUCTURE_1b5o| PDB=1b5o | SCENE= }}
{{STRUCTURE_1b5o| PDB=1b5o | SCENE= }}
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'''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1'''
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===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE 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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11432784}}
==About this Structure==
==About this Structure==
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[[Category: Aminotransferase]]
[[Category: Aminotransferase]]
[[Category: Pyridoxal enzyme]]
[[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 Mon Jun 30 18:19:24 2008''

Revision as of 15:19, 30 June 2008

Image:1b5o.png

Template:STRUCTURE 1b5o

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1

Template:ABSTRACT PUBMED 11432784

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 Mon Jun 30 18:19:24 2008

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