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Ribozymes

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...

Hydrolysis of ATP

Hydrolysis of ATP

The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

Nucleic Acid Structure

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...

The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

ATP Synthase: Structure

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...

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Related Experiment Video

Updated: Dec 29, 2025

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

(ADP-ribosyl)hydrolases: structure, function, and biology.

Johannes Gregor Matthias Rack¹, Luca Palazzo², Ivan Ahel¹

¹Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.

Genes & Development

|February 8, 2020

Summary

This summary is machine-generated.

ADP-ribosylation is a key cellular process regulated by (ADP-ribosyl)hydrolases. These enzymes are vital for ADP-ribosyl signaling, impacting health and disease, and offer therapeutic potential.

Keywords:

ADP-ribose ADP-ribosylation ARH3 DNA damage DraG PARG PARP catalytic mechanism genome stability macrodomain structural biology

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Area of Science:

Biochemistry
Molecular Biology
Cellular Signaling

Background:

ADP-ribosylation is a complex posttranslational modification regulating diverse cellular processes.
It involves various chemical linkages to amino acids and nucleic acids.
Understanding these modifications is crucial for cellular function.

Purpose of the Study:

To review the families of (ADP-ribosyl)hydrolases.
To discuss their molecular functions and physiological roles.
To explore their impact on human health and disease.

Main Methods:

Literature review of (ADP-ribosyl)hydrolase families.
Analysis of molecular functions and physiological roles.
Investigation of links to human health and disease.

Main Results:

Identified diverse families of (ADP-ribosyl)hydrolases.
Detailed their specific molecular functions and physiological relevance.
Highlighted their involvement in human health and disease states.

Conclusions:

(ADP-ribosyl)hydrolases are essential components of ADP-ribosyl signaling pathways.
These enzymes represent promising targets for novel therapeutic strategies.
Further research will deepen the understanding of ADP-ribosylation.