Creatininase

In enzymology, a creatininase (EC 3.5.2.10) is an enzyme that catalyses the hydrolysis of creatinine to creatine, which can then be metabolised to urea and sarcosine by creatinase.

creatinine + H₂O

\rightleftharpoons

creatine

Thus, the two substrates of this enzyme are creatinine and H₂O, whereas its product is creatine.

Creatininase is a member of the urease-related amidohydrolases, the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism.

Structural studies

Creatininase from Pseudomonas putida has a core structure consisting of 3-layers, alpha/beta/alpha.

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1J2T, 1J2U, 1Q3K, and 1V7Z.

References

PDB: 3NO4; Joint Center for Structural Genomics (2010). "Crystal structure of a creatinine amidohydrolase (Npun_F1913) from Nostoc punctiforme PCC 73102 at 2.00 A resolution". doi:10.2210/pdb3no4/pdb. {{cite journal}}: Cite journal requires |journal= (help)
Yamamoto K, Oka M, Kikuchi T, Emi S (1995). "Cloning of the creatinine amidohydrolase gene from Pseudomonas sp. PS-7". Biosci. Biotechnol. Biochem. 59 (7): 1331–1332. doi:10.1271/bbb.59.1331. PMID 7670196.
Yoshimoto T, Tanaka N, Kanada N, Inoue T, Nakajima Y, Haratake M, Nakamura KT, Xu Y, Ito K (March 2004). "Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism". J. Mol. Biol. 337 (2): 399–416. doi:10.1016/j.jmb.2004.01.022. PMID 15003455.

Tsuru D, Oka I, Yoshimoto T (1976). "Creatinine decomposing enzymes in Pseudomonas putida". Agric. Biol. Chem. 40 (5): 1011–1018. doi:10.1271/bbb1961.40.1011.

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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