Creatininase is a member of the urease-related amidohydrolases,[2] 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.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1J2T, 1J2U, 1Q3K, and 1V7Z.
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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)
↑ 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. PMID15003455.
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