Quantitative Enzymology

David J. Timson

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Accurate measurement of the quantitative aspects of enzyme-catalysed reactions
is critical for a deeper understanding of their mechanisms, for their exploitation in biotechnology and for targeting enzymes by drug-like molecules. It is important to move beyond basic enzyme kinetics as encapsulated in the Michaelis-Menten equation. The type and magnitude of inhibition should be determined. Since the majority of enzyme-catalysed reactions involve more than one substrate, it is critical to understand how to treat these reactions quantitatively and how their kinetic behaviour depends on the type of mechanism occurring.
Some reactions do not conform to “standard” Michaelis-Menten treatment and exhibit phenomena such as cooperativity. Again it is important to put these phenomena onto a quantitative basis. Similarly the treatment of the effects of pH on enzymes is often vague and uninformative without a proper quantitative treatment. This review brings together tools and approaches for dealing with enzymes quantitatively together with original references for these approaches.
Original languageEnglish
Pages (from-to)12-31
Number of pages20
JournalCurrent Enzyme Inhibition
Volume11
Issue number1
DOIs
Publication statusPublished - 01 Jul 2015

Fingerprint

Enzymes
Enzyme kinetics
Biotechnology
Drug Delivery Systems
Therapeutics
Molecules
Substrates
Pharmaceutical Preparations

Cite this

Timson, David J. / Quantitative Enzymology. In: Current Enzyme Inhibition . 2015 ; Vol. 11, No. 1. pp. 12-31.
@article{f356d9acc2f242d6adfe3eb9ec8046b1,
title = "Quantitative Enzymology",
abstract = "Accurate measurement of the quantitative aspects of enzyme-catalysed reactionsis critical for a deeper understanding of their mechanisms, for their exploitation in biotechnology and for targeting enzymes by drug-like molecules. It is important to move beyond basic enzyme kinetics as encapsulated in the Michaelis-Menten equation. The type and magnitude of inhibition should be determined. Since the majority of enzyme-catalysed reactions involve more than one substrate, it is critical to understand how to treat these reactions quantitatively and how their kinetic behaviour depends on the type of mechanism occurring.Some reactions do not conform to “standard” Michaelis-Menten treatment and exhibit phenomena such as cooperativity. Again it is important to put these phenomena onto a quantitative basis. Similarly the treatment of the effects of pH on enzymes is often vague and uninformative without a proper quantitative treatment. This review brings together tools and approaches for dealing with enzymes quantitatively together with original references for these approaches.",
author = "Timson, {David J.}",
year = "2015",
month = "7",
day = "1",
doi = "10.2174/157340801101150707124226",
language = "English",
volume = "11",
pages = "12--31",
journal = "Current Enzyme Inhibition",
issn = "1573-4080",
publisher = "Bentham Science Publishers B.V.",
number = "1",

}

Quantitative Enzymology. / Timson, David J.

In: Current Enzyme Inhibition , Vol. 11, No. 1, 01.07.2015, p. 12-31.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Quantitative Enzymology

AU - Timson, David J.

PY - 2015/7/1

Y1 - 2015/7/1

N2 - Accurate measurement of the quantitative aspects of enzyme-catalysed reactionsis critical for a deeper understanding of their mechanisms, for their exploitation in biotechnology and for targeting enzymes by drug-like molecules. It is important to move beyond basic enzyme kinetics as encapsulated in the Michaelis-Menten equation. The type and magnitude of inhibition should be determined. Since the majority of enzyme-catalysed reactions involve more than one substrate, it is critical to understand how to treat these reactions quantitatively and how their kinetic behaviour depends on the type of mechanism occurring.Some reactions do not conform to “standard” Michaelis-Menten treatment and exhibit phenomena such as cooperativity. Again it is important to put these phenomena onto a quantitative basis. Similarly the treatment of the effects of pH on enzymes is often vague and uninformative without a proper quantitative treatment. This review brings together tools and approaches for dealing with enzymes quantitatively together with original references for these approaches.

AB - Accurate measurement of the quantitative aspects of enzyme-catalysed reactionsis critical for a deeper understanding of their mechanisms, for their exploitation in biotechnology and for targeting enzymes by drug-like molecules. It is important to move beyond basic enzyme kinetics as encapsulated in the Michaelis-Menten equation. The type and magnitude of inhibition should be determined. Since the majority of enzyme-catalysed reactions involve more than one substrate, it is critical to understand how to treat these reactions quantitatively and how their kinetic behaviour depends on the type of mechanism occurring.Some reactions do not conform to “standard” Michaelis-Menten treatment and exhibit phenomena such as cooperativity. Again it is important to put these phenomena onto a quantitative basis. Similarly the treatment of the effects of pH on enzymes is often vague and uninformative without a proper quantitative treatment. This review brings together tools and approaches for dealing with enzymes quantitatively together with original references for these approaches.

U2 - 10.2174/157340801101150707124226

DO - 10.2174/157340801101150707124226

M3 - Article

VL - 11

SP - 12

EP - 31

JO - Current Enzyme Inhibition

JF - Current Enzyme Inhibition

SN - 1573-4080

IS - 1

ER -