(Q58979166)

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Substrate Hydrophobic Groups and the Maximal Rate of Enzyme Reactions

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Substrate Hydrophobic Groups and the Maximal Rate of Enzyme Reactions (English)

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BAREND H. J. HOFSTEE

1

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English

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publication date

January 1967

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published in

Nature

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volume

213

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page(s)

42-44

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issue

5071

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exact match

https://scigraph.springernature.com/pub.10.1038/213042a0

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cites work

Fatty acid esters as substrates for trypsin and chymotrypsin

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Kinetics of chymotrypsin with a homologous series of n-fatty acid esters as substrates

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SOME ASPECTS OF THE SPECIFICITY OF FATTY ACID ESTERASES.

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Synthesis of some esters of hippuric acid, and their hydrolysis by α-chymotrypsin

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THE PRIMARY SPECIFICITY OF ALPHA-CHYMOTRYPSIN. ACYLATED AMINO ACID ESTERS WITH NORMAL ALKYL SIDE CHAINS

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The relationship of enzyme inhibitory activity to the structure of n-alkylphosphonate and phenylalkyl-phosphonate esters

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Micelle formation in substrates of esterases

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An interpretation of the kinetic behavior of model substrates of alpha-chymotrypsin

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10.1038/213042A0

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1018569420

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(Q58979166)

Substrate Hydrophobic Groups and the Maximal Rate of Enzyme Reactions

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