Creatininase

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Creatininase
3NO4.png
Crystallographic structure of a creatinine amidohydrolase from Nostoc pruniforme.[1]
Identifiers
EC number 3.5.2.10
CAS number 9025-13-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Creatininase
PDB 1v7z EBI.jpg
creatininase-product complex
Identifiers
Symbol Creatininase
Pfam PF02633
InterPro IPR003785
SCOP 1v7z
SUPERFAMILY 1v7z

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 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,[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.

Structural studies[edit]

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

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

References[edit]

  1. ^ 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. 
  2. ^ 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. PMID 7670196. doi:10.1271/bbb.59.1331. 
  3. ^ 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. PMID 15003455. doi:10.1016/j.jmb.2004.01.022. 
  • Tsuru D, Oka I & Yoshimoto T (1976). "Creatinine decomposing enzymes in Pseudomonas putida". Agric. Biol. Chem. 40: 1011–1018. doi:10.1271/bbb1961.40.1011.