Allantoinase

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allantoinase
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Allantoinase (analog) tetramer, Pseudomonas fluorescens
Identifiers
EC no. 3.5.2.5
CAS no. 9025-20-1
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MetaCyc metabolic pathway
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In enzymology, an allantoinase (EC 3.5.2.5) is an enzyme that catalyzes the chemical reaction

(S)-allantoin + H2O allantoate

Thus, the two substrates of this enzyme are (S)-allantoin and H2O, whereas its product is allantoate.

This enzyme belongs to 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 (S)-allantoin amidohydrolase. This enzyme participates in purine metabolism.

Related Research Articles

In biochemistry, a ligase is an enzyme that can catalyze the joining (ligation) of two molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds. For example, DNA ligase can join two complementary fragments of nucleic acid by forming phosphodiester bonds, and repair single stranded breaks that arise in double stranded DNA during replication.

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References


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