1yoo
From Proteopedia
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| - | [[Image:1yoo.jpg|left|200px]] | + | [[Image:1yoo.jpg|left|200px]] |
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| - | '''ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID''' | + | {{Structure |
| + | |PDB= 1yoo |SIZE=350|CAPTION= <scene name='initialview01'>1yoo</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=IVA:ISOVALERIC ACID'>IVA</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YOO is a [ | + | 1YOO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOO OCA]. |
==Reference== | ==Reference== | ||
| - | Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:[http:// | + | Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9891001 9891001] |
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:35 2008'' |
Revision as of 13:25, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID
Overview
Directed evolution was used to change the substrate specificity of aspartate aminotransferase. A mutant enzyme with 17 amino acid substitutions was generated that shows a 2.1 x 10(6)-fold increase in the catalytic efficiency (kcat/Km) for a non-native substrate, valine. The absorption spectrum of the bound coenzyme, pyridoxal 5'-phosphate, is also changed significantly by the mutations. Interestingly, only one of the 17 residues appears to be able to contact the substrate, and none of them interact with the coenzyme. The three-dimensional structure of the mutant enzyme complexed with a valine analog, isovalerate (determined to 2.4-A resolution by x-ray crystallography), provides insights into how the mutations affect substrate binding. The active site is remodeled; the subunit interface is altered, and the enzyme domain that encloses the substrate is shifted by the mutations. The present results demonstrate clearly the importance of the cumulative effects of residues remote from the active site and represent a new line of approach to the redesign of enzyme activity.
About this Structure
1YOO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:9891001
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