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Enzyme Kinetics

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

Introduction to Enzyme Kinetics

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...

Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

Most enzymes...

Enzymes

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

Introduction to Enzymes

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...

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Related Experiment Video

Updated: Feb 24, 2026

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

Network design and analysis for multi-enzyme biocatalysis.

Lisa Katharina Blaß¹, Christian Weyler¹, Elmar Heinzle²

¹Biochemical Engineering Institute, Saarland University, Campus A1.5, Saarbrücken, 66123, Germany.

BMC Bioinformatics

|August 12, 2017

Summary

Designing multi-step biosynthesis pathways is complex. We developed a computational tool using a pan-organism metabolic network to find optimal enzymatic routes for valuable product synthesis.

Keywords:

Biocatalysis Mixed-integer linear program Multi-enzyme catalysis Network analysis Network design Path-finding Pathway Side reactions Synthetic biology Thermodynamics

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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

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Area of Science:

Biotechnology
Synthetic Biology
Metabolic Engineering

Background:

Designing multi-step biosynthesis pathways for valuable products is increasingly complex due to vast biological data.
Manual design of enzymatic routes involving enzymes from different organisms is challenging.

Purpose of the Study:

To develop a computational tool for directed design of biosynthetic production pathways.
To enable multi-step catalysis using in vitro enzyme cascades, cell hydrolysates, and permeabilized cells.

Main Methods:

Reconstruction of a genome-scale pan-organism metabolic network using KEGG and eQuilibrator data.
Implementation of a mixed-integer linear program (MILP) path-finding algorithm considering network topology and stoichiometry.
Pathway candidate ranking based on biochemical criteria like length, thermodynamics, and cofactor requirements.

Main Results:

A method for proposing suitable synthesis pathways from arbitrary starting metabolites to a target product.
Generation of pathway alternatives with thermodynamic profiles, reactant balances, and potential side reactions.
Output includes an SBML file for pathway visualization.

Conclusions:

An in silico tool for designing multi-enzyme biosynthetic pathways from a pan-organism network is presented.
The method is highly customizable and adaptable to specific project needs.
Applicable to in vitro enzyme cascades, cell hydrolysates, and permeabilized cells.