Creatininase
Creatininase[edit | edit source]
Creatininase is an enzyme that catalyzes the conversion of creatinine to creatine. This enzyme is part of the hydrolase family, specifically those acting on carbon-nitrogen bonds other than peptide bonds, in linear amidines. Creatininase plays a crucial role in the creatinine degradation pathway, which is important for the regulation of creatine and creatinine levels in the body.
Function[edit | edit source]
Creatininase facilitates the hydrolysis of creatinine to creatine, which can then be further metabolized to sarcosine and urea by the action of other enzymes such as creatine amidinohydrolase and sarcosine oxidase. This enzymatic activity is essential for maintaining the balance of creatinine in the body, which is a waste product of muscle metabolism and is excreted in the urine.
Structure[edit | edit source]
Creatininase is a protein that typically forms a homodimer, meaning it consists of two identical subunits. The enzyme's active site is responsible for binding creatinine and facilitating its conversion to creatine. The structure of creatininase has been elucidated through X-ray crystallography, revealing details about its active site and substrate binding.
Mechanism[edit | edit source]
The enzymatic mechanism of creatininase involves the nucleophilic attack on the carbon atom of the creatinine ring, leading to the opening of the ring and formation of creatine. This reaction is facilitated by the presence of a water molecule, which acts as a nucleophile, and specific amino acid residues in the active site that stabilize the transition state.
Clinical Significance[edit | edit source]
The activity of creatininase is of clinical importance in the measurement of creatinine levels in blood and urine, which are used as indicators of kidney function. Abnormal levels of creatinine can indicate renal impairment or other metabolic disorders. Enzymatic assays utilizing creatininase are commonly employed in clinical laboratories to assess creatinine concentrations.
Industrial Applications[edit | edit source]
Creatininase is used in various biotechnological applications, particularly in the development of biosensors for the detection of creatinine in biological samples. These biosensors are valuable tools in clinical diagnostics and point-of-care testing.
Related pages[edit | edit source]
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates, categories Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD