Methylamine dehydrogenase (amicyanin)
| Methylamine dehydrogenase (amicyanin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.9.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Methylamine dehydrogenase (amicyanin) (EC 1.4.9.1, MADH, amine dehydrogenase, primary-amine dehydrogenase, methylamine:amicyanin oxidoreductase (deaminating)) catalyzes the reduction of copper-dependent electron-carrier amicyanin via oxidation of methylamine to formaldehyde.[1][2][3][4][5]
This reaction requires the post-translational formation of a tryptophan tryptophylquinone (TTQ) cofactor.[6] MADH forms a tetramer of two light-chain and two heavy-chain protomers. The TTQ cofactor is located in the light-chain and is formed from oxidative coupling between Trp57 and Trp108 (Paracoccus denitrificans numbering) catalyzed by the diheme enzyme MauG.[6]
In P. denitrificans, methylamine dehydrogenase transiently forms a ternary complex to catalyze methylamine-dependent cytochrome c-551i reduction.[7] Within this complex, electrons are transferred from the TTQ cofactor of MADH to the Type 1 copper center of amicyanin, and then to the heme of the cytochrome.
References
- ^ de Beer R, Duine JA, Frank J, Large PJ (April 1980). "The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure". Biochimica et Biophysica Acta. 622 (2): 370–4. doi:10.1016/0005-2795(80)90050-1. PMID 6246962.
- ^ Eady RR, Large PJ (January 1968). "Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine". The Biochemical Journal. 106 (1): 245–55. doi:10.1042/bj1060245. PMC 1198491. PMID 4388687.
- ^ Eady RR, Large PJ (August 1971). "Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1". The Biochemical Journal. 123 (5): 757–71. doi:10.1042/bj1230757. PMC 1177077. PMID 5124384.
- ^ Cavalieri C, Biermann N, Vlasie MD, Einsle O, Merli A, Ferrari D, Rossi GL, Ubbink M (June 2008). "Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus". Biochemistry. 47 (25): 6560–70. doi:10.1021/bi7023749. PMID 18512962.
- ^ Meschi F, Wiertz F, Klauss L, Cavalieri C, Blok A, Ludwig B, Heering HA, Merli A, Rossi GL, Ubbink M (October 2010). "Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex". Journal of the American Chemical Society. 132 (41): 14537–45. Bibcode:2010JAChS.13214537M. doi:10.1021/ja105498m. hdl:11381/2328147. PMID 20873742.
- ^ a b Jensen, Lyndal M. R.; Sanishvili, Ruslan; Davidson, Victor L.; Wilmot, Carrie M. (2010). "In Crystallo Posttranslational Modification Within a MauG/Pre–Methylamine Dehydrogenase Complex". Science. 327 (5971): 1392–1394. doi:10.1126/science.1182492. PMC 2878131. PMID 20223990.
- ^ Davidson VL (August 2004). "Electron transfer in quinoproteins". Archives of Biochemistry and Biophysics. 428 (1): 32–40. doi:10.1016/j.abb.2004.03.022. PMID 15234267.
External links
- methylamine+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)