Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Pyruvate Oxidation

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...

Urea Cycle

Urea Cycle

The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.

Erythropoiesis

Erythropoiesis

Red blood cells (RBCs) transport oxygen to all body tissues. These cells survive only for 120 days and then need to be replenished. Erythropoiesis is the process of RBC production. In healthy individuals, erythropoiesis ensures all tissues are amply supplied with oxygen. In addition, blood loss due to injury leads to a drop in the physiological oxygen level that will cause erythropoiesis. Any defect in erythropoiesis leads to several physiological disorders, including thalassemia, anemia, and...

Electron Transport Chain: Complex III and IV

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

Erythropoiesis

Erythropoiesis

Red blood cells (RBCs) transport oxygen to all body tissues. These cells survive only for 120 days and then need to be replenished. Erythropoiesis is the process of RBC production. In healthy individuals, erythropoiesis ensures all tissues are amply supplied with oxygen. In addition, blood loss due to injury leads to a drop in the physiological oxygen level that will cause erythropoiesis. Any defect in erythropoiesis leads to several physiological disorders, including thalassemia, anemia, and...

Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes

Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes

Cytochrome P450 (CYP450) enzymes are a superfamily of heme-containing monooxygenases that play a pivotal role in Phase I drug metabolism by catalyzing oxidation and reduction reactions.These enzymes transform lipophilic xenobiotics into more hydrophilic metabolites, facilitating subsequent Phase II conjugation and eventual excretion. The CYP450 family is classified into families (e.g., CYP1–CYP3) and subfamilies (e.g., CYP2A, CYP2C), based on amino acid sequence homology.CYP450 isoenzymes,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The effects of anthracycline drugs on the conformational distribution of mouse P-glycoprotein explains their transport rate differences.

Biochemical pharmacology·2020

Same author

The conformation and dynamics of P-glycoprotein in a lipid bilayer investigated by atomic force microscopy.

Biochemical pharmacology·2018

Same author

Linking economic hardship to adolescent aggression.

Journal of youth and adolescence·2013

Same author

Tolerability of combined treatment with lithium and paroxetine: 19 cases treated under open conditions.

Journal of psychopharmacology (Oxford, England)·2012

Same author

Characterization of a large genomic deletion in four Irish families with C7 deficiency.

Molecular immunology·2011

Same author

Plasmodesmal targeting and intercellular movement of potato mop-top pomovirus is mediated by a membrane anchored tyrosine-based motif on the lumenal side of the endoplasmic reticulum and the C-terminal transmembrane domain in the TGB3 movement protein.

Virology·2010

Search research articles

Related Experiment Video

Updated: Jul 15, 2026

Light-driven Enzymatic Decarboxylation

Light-driven Enzymatic Decarboxylation

Published on: May 22, 2016

Uroporphyrinogen decarboxylase

G H Elder¹, A G Roberts

¹Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, England.

Journal of Bioenergetics and Biomembranes

|April 1, 1995

Summary

Uroporphyrinogen decarboxylase is crucial for preventing uroporphyria. Its deficiency, due to genetic or environmental factors like aromatic hydrocarbons, causes human porphyrias.

Area of Science:

Biochemistry
Enzymology
Toxicology

Background:

Uroporphyrinogen decarboxylase (EC 4.1.1.37) catalyzes a key step in heme biosynthesis.
Enzymes from various species share similar characteristics, yet structure-function relationships remain largely unelucidated.
Hepatic uroporphyria is induced by aromatic hydrocarbons, which reduce enzyme activity.

Purpose of the Study:

Review the roles of inherited and acquired factors in human and experimental uroporphyrias.
Discuss the pathogenesis of porphyria cutanea tarda and hepatoerythropoietic porphyria.
Highlight the significance of uroporphyrinogen decarboxylase activity.

Main Methods:

Literature review of biochemical and toxicological studies.
Analysis of enzyme kinetics and physicochemical properties.

More Related Videos

Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling

Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by ³²P-postlabeling

Published on: March 20, 2018

Porphyrin-Modified Beads for Use as Compensation Controls in Flow Cytometry

Porphyrin-Modified Beads for Use as Compensation Controls in Flow Cytometry

Published on: March 24, 2023

Related Experiment Videos

Last Updated: Jul 15, 2026

Light-driven Enzymatic Decarboxylation

Light-driven Enzymatic Decarboxylation

Published on: May 22, 2016

Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling

Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by ³²P-postlabeling

Published on: March 20, 2018

Porphyrin-Modified Beads for Use as Compensation Controls in Flow Cytometry

Porphyrin-Modified Beads for Use as Compensation Controls in Flow Cytometry

Published on: March 24, 2023

Examination of genetic and environmental factors in porphyria.

Main Results:

Uroporphyrinogen decarboxylase deficiency underlies major human porphyrias.
Aromatic hydrocarbons decrease hepatic enzyme activity, leading to uroporphyria.
Iron is implicated as a factor in porphyria pathogenesis.

Conclusions:

Uroporphyrinogen decarboxylase is a critical enzyme in heme metabolism.
Understanding enzyme structure-function is vital for treating porphyrias.
Both genetic predisposition and environmental exposures contribute to uroporphyria development.