Domain

Creatinase, N-terminal (IPR000587)

Short name: Creatinase_N

Overlapping homologous superfamilies

Domain relationships

None.

Description

Creatinase or creatine amidinohydrolase (EC:3.5.3.3) catalyses the conversion of creatine and water to sarcosine and urea. The enzyme works as a homodimer, and is induced by choline chloride. Each monomer of creatinase has two clearly defined domains, a small N-terminal domain, and a large C-terminal domain.

The structure of the C-terminal region represents the "pita-bread" fold. The fold contains both alpha helices and an anti-parallel beta sheet within two structurally similar domains that are thought to be derived from an ancient gene duplication. The active site, where conserved, is located between the two domains. The fold is common to methionine aminopeptidase (EC:3.4.11.18), aminopeptidase P (EC:3.4.11.9), prolidase (EC:3.4.13.9), agropine synthase and creatinase (EC:3.5.3.3). Though many of these peptidases require a divalent cation, creatinase is not a metal-dependent enzyme [PMID: 8146141, PMID: 12136144, PMID: 8471602].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016787 hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam