ArticleApplied and environmental microbiology2011
Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 23 citations in OpenAlex.
- Design and development of spectrophotometric enzymatic cyanide assays.Analytical and bioanalytical chemistry · 2025Article
- Microbial amidases: Characterization, advances and biotechnological applications.Biotechnology notes (Amsterdam, Netherlands) · 2025Review
- Prospects of formamide as nitrogen source in biotechnological production processes.Applied microbiology and biotechnology · 2024Review
- Different ways to transport ammonia in human and Mycobacterium tuberculosis NADNature communications · 2020Article
- Crystal structure of E. coli apolipoprotein N-acyl transferase.Nature communications · 2017Article
- Purification and characterization of a thermostable aliphatic amidase from the hyperthermophilic archaeon Pyrococcus yayanosii CH1.Extremophiles : life under extreme conditions · 2014Article
- The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.The Journal of biological chemistry · 2013Article
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8 authors at 2 institutions in 1 country.
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Abstract
Formamidases (EC 3.5.1.49) are poorly characterized proteins. In spite of this scarce knowledge, ammonia has been described as playing a central role in the pathogenesis of human pathogens such as Helicobacter pylori, for which formamidase has been shown to participate in the nitrogen metabolic pathway. Sequence analysis has revealed that at least two different groups of formamidases are classified as EC 3.5.1.49: on the one hand, the derivatives of the FmdA-AmdA superfamily, which are the best studied to date, and on the other hand, the derivatives of Helicobacter pylori AmiF. Here we present the cloning, purification, and characterization of a recombinant formamidase from Bacillus cereus CECT 5050T (BceAmiF), the second member of the AmiF subfamily to be characterized, showing new features of the enzyme further supporting its relationship with aliphatic amidases. We also present homology modeling-based mutational studies confirming the importance of the Glu140 and Tyr191 residues in the enzymatic activities of the AmiF family. Moreover, we can conclude that a second glutamate residue is critical in several members of the nitrilase superfamily, meaning that what has consistently been identified as a C-E-K triad is in fact a C-E-E-K tetrad.
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