Biology:Formamidase
Formamidase (EC 3.5.1.49) is an enzyme characterised from Pseudomonas aeruginosa and Alcaligenes eutrophus that catalyzes the chemical reaction which hydrolyses formamide to formic acid and ammonia:[1][2]
- REDIRECT Template:Chemical reaction
The formamide binding site in Helicobacter pylori consists of a cysteine-glutamate-lysine catalytic triad.[3] Metabolic engineering techniques have been used to create organisms that can use formamide as sole nitrogen source and hence manufacture useful organic amines from it.[4]
This enzyme is a hydrolase, one acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formamide amidohydrolase.[5]
Structural studies
As of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes 2DYU, 2DYV, 2E2K, and 2E2L.
References
- ↑ Clarke, Patricia H. (1969). "The Aliphatic Amidases of Pseudomonas aeruginosa". Advances in Microbial Physiology Volume 4. 4. pp. 179–222. doi:10.1016/S0065-2911(08)60442-7. ISBN 978-0-12-027704-9.
- ↑ Friedrich, C. G.; Mitrenga, G. (1981). "Utilization of Aliphatic Amides and Formation of Two Different Amidases by Alcaligenes eutrophus". Microbiology 125 (2): 367–374. doi:10.1099/00221287-125-2-367.
- ↑ Hung, Chiu-Lien; Liu, Jia-Hsin; Chiu, Wei-Chun; Huang, Shao-Wei; Hwang, Jenn-Kang; Wang, Wen-Ching (2007). "Crystal Structure of Helicobacter pylori Formamidase AmiF Reveals a Cysteine-Glutamate-Lysine Catalytic Triad". Journal of Biological Chemistry 282 (16): 12220–12229. doi:10.1074/jbc.M609134200. PMID 17307742.
- ↑ Schwardmann, Lynn S.; Wu, Tong; Dransfeld, Aron K.; Lindner, Steffen N.; Wendisch, Volker F. (2023). "Formamide-based production of amines by metabolically engineering Corynebacterium glutamicum". Applied Microbiology and Biotechnology 107 (13): 4245–4260. doi:10.1007/s00253-023-12592-3. PMID 37246985.
- ↑ Enzyme 3.5.1.49 at KEGG Pathway Database.
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