1cq6: Difference between revisions

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[[Image:1cq6.jpg|left|200px]]
{{Seed}}
[[Image:1cq6.png|left|200px]]


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{{STRUCTURE_1cq6|  PDB=1cq6  |  SCENE=  }}  
{{STRUCTURE_1cq6|  PDB=1cq6  |  SCENE=  }}  


'''ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE'''
===ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE===




==Overview==
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Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement.
The line below this paragraph, {{ABSTRACT_PUBMED_10858450}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10858450 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10858450}}


==About this Structure==
==About this Structure==
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[[Category: Nakai, T.]]
[[Category: Nakai, T.]]
[[Category: Enzyme-substrate complex]]
[[Category: Enzyme-substrate complex]]
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