1c9c

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{{STRUCTURE_1c9c| PDB=1c9c | SCENE= }}
{{STRUCTURE_1c9c| PDB=1c9c | SCENE= }}
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'''ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE'''
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===ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE===
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==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.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:24:01 2008''

Revision as of 17:24, 30 June 2008

Template:STRUCTURE 1c9c

ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE

Template:ABSTRACT PUBMED 10858450

About this Structure

1C9C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Free energy requirement for domain movement of an enzyme., Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S, J Biol Chem. 2000 Jun 23;275(25):18939-45. PMID:10858450

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