An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5- deazariboflavin

Biochemistry

Volumn 48, Issue 19, 2009, Pages 4181-4188

  Grochowski, Laura L ^a   Xu, Huimin ^a   White, Robert H ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEA; ARCHAEAL; BACTERIAL PATHWAY; BIOSYNTHETIC PATHWAY; FERROUS IRON; FORMAMIDE; FORMYL GROUP; GTP CYCLOHYDROLASE; HYDROLASE; MONOPHOSPHATE; PURIFIED PROTEIN;

AMIDES; AMINES; BACTERIOLOGY; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; IRON; IRON ANALYSIS; METAL REFINING; ZINC;

FOOD ADDITIVES;

7,8 DINOR 8 HYDROXY 5 DEAZARIBOFLAVIN; BACTERIAL ENZYME; FERROUS ION; FORMAMIDE HYDROLASE; FORMIC ACID; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE I; HYDROLASE; PHOSPHATE; PROTEIN ARFB; RIBOFLAVIN; RIBOFLAVIN DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; BIOSYNTHESIS; CONTROLLED STUDY; ENZYME ACTIVITY; METHANOCOCCUS JANNASCHII; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BIOSYNTHETIC PATHWAYS; CATALYSIS; FORMAMIDES; GTP CYCLOHYDROLASE; GUANOSINE TRIPHOSPHATE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; IRON; KINETICS; METHANOCOCCACEAE; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PYRIMIDINONES; RIBOFLAVIN; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; BACTERIA (MICROORGANISMS); EUKARYOTA; METHANOCALDOCOCCUS JANNASCHII;

EID: 66049090396     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802341p     Document Type: Article

References (31)

1. Johnson, E. F., and Mukhopadhyay, B. (2005) A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii. J. Biol. Chem. 280, 38776-38786. (Pubitemid 43853780)
2. 2 detoxification. Arch. Microbiol. 182, 126-137.
3. 2O. FEBS J. 274, 1588-1599.
4. Eker, A. P., Kooiman, P., Hessels, J. K., and Yasui, A. (1990) DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265, 8009-8015. (Pubitemid 20158974)
5. Michel, R., Massanz, C., Kostka, S., Richter, M., and Fiebig, K. (1995) Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 233, 727-735.
6. Jacobson, F. S., Daniels, L., Fox, J. A., Walsh, C. T., and Orme-Johnson, W. H. (1982) Purification and properties of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum. J. Biol. Chem. 257, 3385-3388. (Pubitemid 12077124)
7. Fox, J. A., Livingston, D. J., Orme-Johnson, W. H., and Walsh, C. T. (1987) 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum. 1. Purification and characterization. Biochemistry 26, 4219-4227.
8. Graupner, M., Xu, H., and White, R. H. (2002) The pyrimidine nucleotide reductase step in riboflavin and F420 biosynthesis in archaea proceeds by the eukaryotic route to riboflavin. J. Bacteriol. 184, 1952-1957. (Pubitemid 34275539)
9. Romisch-Margl, W., Eisenreich, W., Haase, I., Bacher, A., and Fischer, M. (2008) 2,5-Diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate synthases of fungi and archaea. FEBS J. 275, 4403-4414.
10. Graham, D. E., Xu, H., and White, R. H. (2002) A member of a new class of GTP cyclohydrolases produces formylaminopyrimidine nucleotide monophosphates. Biochemistry 41, 15074-15084. (Pubitemid 35470687)
11. Bracher, A., Schramek, N., and Bacher, A. (2001) Biosynthesis of pteridines. Stopped-flow kinetic analysis of GTP cyclohydrolase I. Biochemistry 40, 7896-7902.
12. Graham, D. E., Xu, H., and White, R. H. (2002) Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes. J. Biol. Chem. 277, 13421-13429.
13. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
14. Graham, D. E., Overbeek, R., Olsen, G. J., and Woese, C. R. (2000) An archaeal genomic signature. Proc. Natl. Acad. Sci. U.S.A. 97, 3304-3308. (Pubitemid 30183297)
15. Koma, D., Sawai, T., Harayama, S., and Kino, K. (2006) Overexpression of the genes from thermophiles in Escherichia coli by high-temperature cultivation. Appl. Microbiol. Biotechnol. 73, 172-180. (Pubitemid 44627739)
16. Beuth, B., Niefind, K., and Schomburg, D. (2003) Crystal structure of creatininase from Pseudomonas putida: a novel fold and a case of convergent evolution. J. Mol. Biol. 332, 287-301.
17. Yoshimoto, T., Tanaka, N., Kanada, N., Inoue, T., Nakajima, Y., Haratake, M., Nakamura, K. T., Xu, Y., and Ito, K. (2004) Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism. J. Mol. Biol. 337, 399-416. (Pubitemid 38293407)
18. Beuth, B., Niefind, K., and Schomburg, D. (2003) Crystal structure of creatininase from Pseudomonas putida: a novel fold and a case of convergent evolution. J. Mol. Biol. 332, 287-301.
19. Yoshimoto, T., Tanaka, N., Kanada, N., Inoue, T., Nakajima, Y., Haratake, M., Nakamura, K. T., Xu, Y., and Ito, K. (2004) Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism. J. Mol. Biol. 337, 399-416. (Pubitemid 38293407)
20. Spoonamore, J. E., and Bandarian, V. (2008) Understanding functional divergence in proteins by studying intragenomic homologues. Biochemistry 47, 2592-2600.
21. Foor, F., and Brown, G. M. (1975) Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J. Biol. Chem. 250, 3545-3551.
22. Rikitake, K., Oka, I., Ando, M., Yoshimoto, T., and Tsuru, D. (1979) Creatinine amidohydrolase (creatininase) from Pseudomonas putida. Purification and some properties. J. Biochem. (Tokyo) 86, 1109-1117.
23. Kyte, J. (1995) Cooperativity, in Mechanism in Protein Chemistry (Kyte, J., Ed.) pp 473-490, Garland Publishing, New York..
24. Ritz, H., Schramek, N., Bracher, A., Herz, S., Eisenreich, W., Richter, G., and Bacher, A. (2001) Biosynthesis of riboflavin: studies on the mechanism of GTP cyclohydrolase II. J. Biol. Chem. 276, 22273-22277.
25. Spoonamore, J. E., Dahlgran, A. L., Jacobsen, N. E., and Bandarian, V. (2006) Evolution of new function in the GTP cyclohydrolase II proteins of Streptomyces coelicolor. Biochemistry 45, 12144-12155.
26. 2+-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii. Biochemistry 46, 6658-6667.
27. Porter, D. J., and Austin, E. A. (1993) Cytosine deaminase. The roles of divalent metal ions in catalysis. J. Biol. Chem. 268, 24005-24011.
28. Rajagolapan, P. T., Yu, X., and Pei, D. (1997) Peptide deformylase: A new type of mononuclear iron protein. J. Am. Chem. Soc. 119, 12418.
29. Gantt, S. L., Gattis, S. G., and Fierke, C. A. (2006) Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry 45, 6170-6178. (Pubitemid 43727109)
30. D'Souza, V, M., and Holz, R. C. (1999) The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry 38, 11079-11085. (Pubitemid 129752905)
31. Dupont, C. L., Yang, S., Palenik, B., and Bourne, P. E. (2006) Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry. Proc. Natl. Acad. Sci. U.S.A. 103, 17822-17827.