Enzyme flexibility: a new concept in recognition of hydrophobic substrates.

Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Research Abstract Details 

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Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Abstract Text:

S Kawaguchi,Y Nobe,J Yasuoka,T Wakamiya,S Kusumoto,S Kuramitsu,

The mechanism of recognition of hydrophobic substrates was investigated using Escherichia coli aspartate aminotransferase (AspAT), E. coli aromatic amino acid aminotransferase (AroAT), and their chimeric enzyme (DY18). Surprisingly, broad substrate specificity was observed in the reaction of aminotransferases with hydrophobic substrates. The catalytic efficiency increased with an increase in the side chain length of straight or branched-terminal aliphatic substrates. The straight-chain substrates catalysed with maximal efficiency were the 7-carbon substrate in the case of AspAT and the 8-carbon substrate for AroAT and DY18. Consecutive addition of single methylene groups to the substrate had a constant effect on the stabilization energy of the transition state relative to the unbound state. The dependency of binding energy on each methylene group is usually interpreted as indicating hydrophobicity of the active site. However, we observed that AroAT and DY18 had different dependencies although both enzymes have the same residues in the substrate-binding pocket. For substrates with more than 7 carbons, the aminotransferases did not strictly distinguish between substrates with straight and branched side chains. These results suggest that the recognition of manifold hydrophobic substrates of different shapes might require not only the hydrophobicity of the active site but also enzyme flexibility.

Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Publishing Authors By Initials

S Kawaguchi,Y Nobe,J Yasuoka,T Wakamiya,S Kusumoto,S Kuramitsu,

For similar enzymes and coenzymes: enzymes: transferases: nitrogenous group transferases: transaminases research abstracts see: enzymes and coenzymes: enzymes: transferases: nitrogenous group transferases: transaminases research

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Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 122

Page Numbers: 55-63

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1997

Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Keywords Mesh Terms:

KEYWORDS: Transaminases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Enzyme flexibility: a new concept in recognition of hydrophobic substrates. Information

Substance Name: aromatic amino acid aminotransferase

Registry Number: EC 2.6.1.57

Grant and Affiliation Information for Enzyme flexibility: a new concept in recognition of hydrophobic substrates.

AFFILIATION: Department of Biology, Graduate School of Science, Osaka University.

Country: JAPAN

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MEDLINETA: J Biochem

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