Amine dehydrogenase

Hacisalihoglu A, JA Jongejan, JA Duine (1997) Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology (UK) 143 505-512. 

An inducible primary amine dehydrogenase in a strain of Mycobacterium convolutum had diverse degradative capability with a broad specificity, and was involved in the degradation of 1- and 2-aminopropane and 1,3-diaminopropane. The products were assimilated by the methylmalonate pathway, or by formation of C2 + Cj fragments (Cerniglia and Perry 1975). 

This enzyme [EC 1.4.99.3], also known as amine dehydrogenase and primary-amine dehydrogenase, catalyzes the reaction of R-CH2-NH2 with water and an acceptor to produce R-CHO, ammonia, and the reduced acceptor. Tryptophan tryptophylquinone (TTQ) is the cofactor for this enzyme. See Resonance Raman Spectroscopy Topaquinone... 

Scheme 6.11 The holy grail an NAD(P)-dependent amine dehydrogenase.

Tryptophan tryptophanylquinone (TTQ). This recently discovered quinone cofactor is similar to the lysyl tyrosylquinone but is formed from two trypto-phanyl side chains.466 It has been found in methyl-amine dehydrogenase from methylotrophic gramnegative bacteria467-469 and also in a bacterial aromatic amine dehydrogenase.470... 

Govindaraj, S., Eisenstein, E., Jones, L. H., Sanders-Loehr, J., Chistoserdov, A. Y., Davidson, V. L., and Edwards, S. L. 1994, Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J. Bacterial. 176 292292929. 

Hyun, Y-L., and Davidson V. L., 1995, Electron transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry 34 12249912254. 

Datta, S. Moei, Y. Takagi, K. Kawaguchi, K. Chen, Z.-W. Okajima, T. Kueoda, S. Ikeda, T. Kano, K. Tanizawa, K., Mathews, F. S. 2001 Proc. Nad. Acad. Sci. USA 98, 14268-14273 Structure of a quino-hemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking. 

H-Tunneling in Flavoprotein Amine Dehydrogenases Heterotetrameric Sarcosine Oxidase and Engineering Gated Motion in Trimethylamine Dehydrogenase... 

Although H-transfer in flavoprotein amine dehydrogenases has been shown to occur by tunneling, the mechanisms of amine oxidation by flavoproteins remain controversial. Over the years mechanisms involving the following have been con-... 

Figure 6 Structure and relative orientations of the CTQ and heme cofactors in quinohemoprotein amine dehydrogenase from P. denitrificans. In this enzyme, oxygenation of 7Trp43 and cross-linking with 7Cys37 yields the CTQ cofactor. CTQ and the two hemes present on the a subunit are displayed as sticks colored gray for carbon, red for oxygen, blue for nitrogen, yellow for sulfur, and dark red for iron. The coordinates from PDB entry 1 pby were used to display this structure.

Scheme 12 The reaction mechanism of CTQ-dependent quinohemoprotein amine dehydrogenase.

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