Guanidinobutyrase

Guanidinobutyrase is an enzyme that catalyzes the chemical reaction of converting 4-guanidinobutanoate to 4-aminobutanoate and urea. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds, in linear amides. The systematic name of this enzyme class is 4-guanidinobutanoate amidinohydrolase.

Function

Guanidinobutyrase plays a crucial role in the metabolism of arginine and proline, two important amino acids. It is involved in the breakdown of arginine, converting it into other substances that the body can use. This process is essential for the removal of excess nitrogen from the body.

Structure

Like other enzymes, guanidinobutyrase is a protein that is folded into a specific three-dimensional shape. This shape allows it to bind to its substrate, the molecule it acts on, and carry out its function. The structure of guanidinobutyrase is not yet fully understood, and research is ongoing to determine its exact form and how it interacts with its substrate.

Clinical Significance

Abnormal levels of guanidinobutyrase can indicate problems with arginine and proline metabolism. This can lead to a variety of health issues, including neurological disorders, kidney disease, and certain types of cancer. Testing for guanidinobutyrase levels can therefore be a useful diagnostic tool in certain situations.

See Also

• Enzyme
• Hydrolase
• Arginine
• Proline
• Metabolism

References

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