Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics.

Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Research Abstract Details 

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Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Abstract Text:

Lei Liu,Mary Rozenman,Ronald Breslow,

The amination of ketoacids to amino acids by pyridoxamine is greatly accelerated when the pyridoxamine is covalently linked to polyethylenimine carrying N-methyl and N-lauryl groups. Michaelis-Menten kinetics is seen with all substrates, from which the effect of the lauryl groups and the methyl groups can be determined with respect to the strength of binding of the substrate and the rate constant k2 within the complex. The polyamine catalyzes the reaction using acid and base groups, the lauryl groups increase k2 by producing a nonpolar medium in which the reaction occurs, and the lauryl groups promote binding of hydrophobic substrates. The result is that the amination of indolepyruvic acid to produce tryptophan is accelerated by 240000-fold.

Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Publishing Authors By Initials

L Liu,M Rozenman,R Breslow,

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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Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of the American Chemical Society

VOLUME: 124

Page Numbers: 12660-1

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 30

MONTH: Oct

YEAR: 2002

Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Keywords Mesh Terms:

KEYWORDS: Transaminases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics. Information

Substance Name: Transaminases

Registry Number: EC 2.6.1.-

Grant and Affiliation Information for Hydrophobic effects on rates and substrate selectivities in polymeric transaminase mimics.

AFFILIATION: Department of Chemistry, Columbia University, New York, New York 10027, USA.

Country: United States

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MEDLINETA: J Am Chem Soc

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