Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis: Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans

FEBS Journal

Volumn 272, Issue 22, 2005, Pages 5894-5909

  Hothi, Parvinder ^a   Khadra, Khalid Abu ^a   Combe, Jonathan P ^a   Leys, David ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Amine oxidation; Aromatic amine dehydrogenase; Cofactor biogenesis; Stopped flow spectroscopy; Tryptophan tryptophyl quinone

Indexed keywords

ARALKYLAMINE DEHYDROGENASE; BENZYLAMINE; OXIDOREDUCTASE; TRYPTAMINE; TRYPTOPHAN DERIVATIVE; TRYPTOPHAN TRYPTOPHYLQUINONE COFACTOR; UNCLASSIFIED DRUG;

ALCALIGENES FAECALIS; ARTICLE; BIOGENESIS; CATALYSIS; CHEMICAL BINDING; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; GENE CLUSTER; IONIZATION; NONHUMAN; OXIDATION; PARACOCCUS DENITRIFICANS; PKA; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; QUANTUM MECHANICS; REGULATORY MECHANISM; STEADY STATE; TEMPERATURE DEPENDENCE;

ALCALIGENES FAECALIS; CATALYSIS; HYDROGEN-ION CONCENTRATION; INDOLEQUINONES; KINETICS; MASS SPECTROMETRY; MOLECULAR STRUCTURE; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PARACOCCUS DENITRIFICANS; RECOMBINANT PROTEINS; TRYPTOPHAN;

ALCALIGENES FAECALIS; PARACOCCUS DENITRIFICANS;

EID: 28044447627     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04990.x     Document Type: Article

References (30)

1. Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL & Edwards SL (1994) Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol 176, 2922-2929.
2. Edwards SL, Davidson VL, Hyun YL & Wingfield PT (1995) Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem 270, 4293-4298.
3. Hyun YL & Davidson VL (1995) Electron transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry 34, 12249-12254.
4. Masgrau L, Roujeinikova A, Johannissen L, Basran J, Ranaghan K, Hothi P, Mulholland A, Sutcliffe M, Scrutton N & Leys D (2005) Atomic description of an enzyme reaction dominated by hydrogen tunnelling, submitted.
5. Vellieux FM, Huitema F, Groendijk H, Kalk KH, Jzn JF, Jongejan JA, Duine JA, Petratos K, Drenth J & Hol WG (1989) Structure of quinoprotein methylamine dehydrogenase at 2.25 Å resolution. EMBO J 8, 2171-2178.
6. McIntire WS, Wemmer DE, Chistoserdov A & Lidstrom ME (1991) A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science 252, 817-824.
7. Chistoserdov AY (2001) Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology 147, 2195-2202.
8. Graichen ME, Jones LH, Sharma BV, van Spanning RJ, Hosler JP & Davidson VL (1999) Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides. J Bacteriol 181, 4216-4222.
9. Jones L, Pearson AR, Tang Y, Wilmot C & Davidson V (2005) J Biol Chem 280, 17392-17396.
10. Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM & Davidson VL (2003) MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry 42, 7318-7325.
11. Pearson AR, De La Mora-Rey T, Graichen ME, Wang Y, Jones LH, Marimanikkupam S, Agger SA, Grimsrud PA, Davidson VL & Wilmot CM (2004) Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation. Biochemistry 43, 5494-5502.
12. van der Palen CJ, Slotboom DJ, Jongejan L, Reijnders WN, Harms N, Duine JA & van Spanning RJ (1995) Mutational analysis of mau genes involved in methylamine metabolism in Paracoccus denitrificans. Eur J Biochem 230, 860-871.
13. van der Palen CJ, Reijnders WN, de Vries S, Duine JA & van Spanning RJ (1997) MauE and MauD proteins are essential in methylamine metabolism of Paracoccus denitrificans. Antonie Van Leeuwenhoek 72, 219-228.
14. van Spanning RJ, Wansell CW, Reijnders WN, Oltmann LF & Stouthamer AH (1990) Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett 275, 217-220.
15. Van Spanning RJ, van der Palen CJ, Slotboom DJ, Reijnders WN, Stouthamer AH & Duine JA (1994) Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator. Eur J Biochem 226, 201-210.
16. Basran J, Sutcliffe MJ & Scrutton NS (1999) Enzymatic H-transfer requires vibration-driven extreme tunneling. Biochemistry 38, 3218-3222.
17. Basran J, Patel S, Sutcliffe MJ & Scrutton NS (2001) Importance of barrier shape in enzyme-catalyzed reactions - Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases. J Biol Chem 276, 6234-6242.
18. Davidson VL (1990) Methylamine dehydrogenase from methylotrophic bacteria. Methods Enzymol 188, 241-246.
19. Ellis KJ & Morrison JF (1982) Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol 87, 405-426.
20. Zhu Z & Davidson VL (1998) Kinetic and chemical mechanisms for the effects of univalent cations on the spectral properties of aromatic amine dehydrogenase Biochem J 329, 175-182.
21. Hyun YL & Davidson VL (1995) Mechanistic studies of aromatic amine dehydrogenase, a tryptophan tryptophylquinone enzyme. Biochemistry 34, 816-823.
22. Kondo T, Kondo E, Maki H, Yasumoto K, Takagi K, Kano K & Ikeda T (2004) Purification and characterization of aromatic amine dehydrogenase from Alcaligenes xylosoxidans. Biosci Biotechnol Biochem 68, 1921-1928.
23. Iwaki M, Yagi T, Horiike K, Saeki Y, Ushijima T & Nozaki M (1983) Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp. Arch Biochem Biophys 220, 253-262.
24. Keen NT, Tamaki S, Kobayashi D & Trollinger D (1988) Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70, 191-197.
25. Sistrom WR (1960) A requirement for sodium in the growth of Rhodopseudomonas spheroids. J Gen Microbiol 22, 778-785.
26. Armstrong MCD (1964) The molecular extinction coefficient of 2,6-dichlorophenol indophenol. Biochim Biophys Acta 86, 194-197.
27. Falzon L & Davidson VL (1996) Kinetic model for the regulation by substrate of intramolecular electron transfer in trimethylamine dehydrogenase. Biochemistry 35, 2445-2452.
28. Basran J, Chohan KK, Sutcliffe MJ & Scrutton NS (2000) Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein. Biochemistry 39, 9188-9200.
29. Harris TK & Davidson VL (1993) A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus denitrificans. Biochemistry 32, 4362-4368.
30. Hothi P, Basran J, Sutcliffe MJ & Scrutton NS (2003) Effects of multiple ligand binding on kinetic isotope effects in PQQ-dependent methanol dehydrogenase. Biochemistry 42, 3966-3978.