Creatinase
Sign in to saveAlso known as creatine amidinohydrolase
In enzymology, creatinase (), also known as creatine amidinohydrolase, is classified as a hydrolase enzyme, acting on carbon-nitrogen bonds in linear amidines. Specifically, this enzyme breaks the amidino C-N bond in creatine, producing sarcosine and urea. Creatinase activity has been described in several bacteria species, most notably Pseudomonas putida, where the enzyme plays a key role in the metabolism of creatine as a nitrogen and carbon source.
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- Commons category
- Creatinase
- EC enzyme number
- 3.5.3.3
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~5 min read
Article
10 sectionsContents
- Organisms and discovery
- Structure
- Domains
- Reaction pathway
- Substrate binding
- Splitting of water
- Breaking the C-N bond and product release
- Importance in metabolism
- Energetics and kinetics
- References
In enzymology, creatinase (), also known as creatine amidinohydrolase, is classified as a hydrolase enzyme, acting on carbon-nitrogen bonds in linear amidines. Specifically, this enzyme breaks the amidino C-N bond in creatine, producing sarcosine and urea. Creatinase activity has been described in several bacteria species, most notably Pseudomonas putida, where the enzyme plays a key role in the metabolism of creatine as a nitrogen and carbon source.
== Organisms and discovery == Creatinase was first identified by Roche, Lacombe, & Girard in 1950 in Pseudomonas eisenbergii and P. ovalis. It is produced by other bacterial genera including Bacillus, Flavobacterium, Micrococcus, Alcaligenes, Clostridium, Arthrobacter, and Paracoccus, and is produced by other species of Pseudomonas as well.