N-formylglutamate deformylase

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In enzymology, a N-formylglutamate deformylase (EC 3.5.1.68) is an enzyme that catalyzes the chemical reaction

N-formyl-L-glutamate + H₂O $\rightleftharpoons$ formate + L-glutamate

Thus, the two substrates of this enzyme are N-formyl-L-glutamate and H₂O, whereas its two products are formate and L-glutamate.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-glutamate amidohydrolase. Other names in common use include beta-citryl-L-glutamate hydrolase, formylglutamate deformylase, N-formylglutamate hydrolase, beta-citrylglutamate amidase, beta-citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate amidase, beta-citrylglutamate amidase, and beta-citryl-L-glutamate-hydrolyzing enzyme. This enzyme participates in histidine metabolism and glyoxylate and dicarboxylate metabolism.

[edit] References

IUBMB entry for 3.5.1.68
BRENDA references for 3.5.1.68 (Recommended.)
PubMed references for 3.5.1.68
PubMed Central references for 3.5.1.68
Google Scholar references for 3.5.1.68
Hu L, Mulfinger LM, Phillips AT (1987). "Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida". J. Bacteriol. 169: 4696–702. PMID 3308850.
Miyake M, Innami T, Kakimoto Y (1983). "A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes". Biochim. Biophys. Acta. 760: 206–14. PMID 6414521.