1CQ7

ASPARTATE AMINOTRANSFERASE (E.C. 2.6.1.1) COMPLEXED WITH C5-PYRIDOXAL-5P-PHOSPHATE

Summary for 1CQ7

• Entry DOI: 10.2210/pdb1cq7/pdb
• Related: 1C9C 1CQ6 1CQ8
• Descriptor: ASPARTATE AMINOTRANSFERASE, 2-[O-PHOSPHONOPYRIDOXYL]-AMINO-PENTANOIC ACID (3 entities in total)
• Functional Keywords: enzyme-substrate complex, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P00509
• Total number of polymer chains: 1
• Total formula weight: 43967.50

Authors

Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S. (deposition date: 1999-08-06, release date: 2000-12-20, Last modification date: 2024-02-07)

Primary citation

Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S.
Free energy requirement for domain movement of an enzyme
J.Biol.Chem., 275:18939-18945, 2000

PubMed Abstract: 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.

PubMed: 10858450
DOI: 10.1074/jbc.275.25.18939

Experimental method

X-RAY DIFFRACTION (2.4 Å)