Sporothrix schenckii: Purification and partial biochemical characterization of glucosamine-6-phosphate synthase, a potential antifungal target

Medical Mycology

Volumn 48, Issue 1, 2010, Pages 110-121

  González Ibarra, Joaquín ^a   Milewski, SŁawomir ^b   Villagómez Castro, Julio C ^a   Cano Canchola, Carmen ^a   López Romero, Everardo ^a  

^a UNIVERSITY OF GUANAJUATO   (Mexico)

^b GDANSK UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

Antifungal target; Glucosamine 6 phosphate synthase; Purifi cation and biochemical characterization; Sporothrix schenckii

Indexed keywords

2 AMINO 2 DEOXY DEXTRO MANNITOL 6 PHOSPHATE; AMINOSUGAR; AMPHOTERICIN B; ENZYME INHIBITOR; FRUCTOSE 6 PHOSPHATE; GLUTAMINE; GLUTAMINE DERIVATIVE; GLUTAMINE FRUCTOSE 6 PHOSPHATE AMINOTRANSFERASE; MANNITOL; N3 (4 METHOXYFUMAROYL) LEVO 2,3 DIAMINOPROPANOIC ACID; UNCLASSIFIED DRUG; URIDINE 5' DIPHOSPHATE N ACETYL DEXTRO GLUCOSAMINE; URIDINE DIPHOSPHATE; VORICONAZOLE; BETA ALANINE; FRUCTOSE PHOSPHATE; FRUCTOSE-6-PHOSPHATE; FUMARIC ACID DERIVATIVE; FUNGAL PROTEIN; MANNOSE; N(3)-(4-METHOXYFUMAROYL)-2,3-DIAMINOPROPIONIC ACID; PROTEIN BINDING; PROTEIN SUBUNIT; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

ARTICLE; CHEMICAL ANALYSIS; CHEMOTHERAPY; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME INHIBITION; FUNGUS GROWTH; ISOELECTRIC POINT; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR WEIGHT; NONHUMAN; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; SPOROTHRIX SCHENCKII; ANALOGS AND DERIVATIVES; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SUBUNIT; SPOROTHRIX;

BETA-ALANINE; ENZYME INHIBITORS; FRUCTOSEPHOSPHATES; FUMARATES; FUNGAL PROTEINS; GLUTAMINE; GLUTAMINE-FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); ISOELECTRIC POINT; KINETICS; MANNOSE; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN SUBUNITS; SPOROTHRIX; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;

FUNGI; SPOROTHRIX SCHENCKII;

EID: 74949124993     PISSN: 13693786     EISSN: 14602709     Source Type: Journal    
DOI: 10.3109/13693780902856030     Document Type: Article

References (61)

1. Bearne SL. Active site-directed inactivation of Escherichia coli glucosamine- 6-phosphate synthase. Determination of the fructose 6-phosphate binding constant using a carbohydrate-based inactivator. J Biol Chem 1996; 271: 3052-3057.
2. Milewski S. Glucosamine-6-phosphate synthase-the multi-facets enzyme. Biochim Biophy Acta 2002; 1597: 173-192.
3. Gabriel I, Olchowy J, Stanislawska-Sachadyn A, et al. Phosphorylation of glucosamine-6-phosphate synthase is important but not essential for germination and mycelial growth of Candida albicans. FEMS Microbiol Lett 2004; 235: 73-80.
4. Hofmann M, Boles E, Zimmermann FK. Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase. Eur J Biochem. 1994; 221: 741-747.
5. Mio T, Yabe T, Arisawa M, Yamada-Okabe H. The eukaryotic UDP-Nacetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. J Biol Chem 1998; 273: 14392-14397.
6. Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H. Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP- N -acetylglucosamine synthesis. J Biol Chem 1999; 274: 424-429.
7. Melcer A, Lacka I, Gabriel I, et al. Rational design of N-alkyl derivatives of 2-amino-2-deoxy-d-glucitol-6P as antifungal agents. Bioorg Med Chem Lett 2007; 17: 6602-6606.
8. Milewski S, Mignini F, Micossi L, Borowski E. Antihistoplasmal in vitro and in vivo effect of Lys-Nva-FMDP. Med Mycol 1998; 36: 177-180.
9. Badet B, Vermoote P, Haumount PY, Lederer F, LeGoffic F. Glucosamine synthetase from Escherichia coli: Purification, properties, and glutamine-utilizing site location. Biochemistry 1987; 26: 1940-1948.
10. Teplyakov A, Obmolova G, Badet P, Badet-Denisot M-A. Channeling of ammonia in glucosamine-6-phosphate synthase. J Mol Biol 2001; 313: 1093-1102.
11. Teplyakov A, Leriche C, Obmolova G, Badet P, Badet-Denisot M-A. From Lobry De Bruyn to enzyme-catalyzed ammonia channelling: molecular studies of D-glucosamine-6P synthase. Nat Prod Rep 2002; 19: 60-69.
12. Durand P, Golinelli-Pimpaneau B, Mouilleron S, Badet B, Badet- Denisot M-A. Highlights of glucosamine-6P synthase catalysis. Arch Biochem Biophys 2008; 474: 302-317.
13. Milewski S, Smith RJ, Brown AJP, Gooday GW. Purification and characterization of glucosamine-6-P synthase from Saccharomyces cerevisiae. In Domard A, Jeuniaux J, Muzzarelli R, Roberts G, (eds). Advances in Chitin Science, vol.1. Lyon: Jacqoues Andre Publishers 1996: 96-101.
14. Milewski S, Kuszczak D, Jedrzejczak R, et al. Oligomeric structure and regulation of Candida albicans glucosamine-6-phosphate synthase. J Biol Chem 1999; 274: 4000-4008.
15. Sachadyn P, Jedrzejczak R, Milewski S, Kur J, Borowski E. Purification to homogeneity of Candida albicans glucosamine-6-phosphate synthase overexpressed in Escherichia coli. Prot Expr Purif 2000; 19: 343-349.
16. Ghosh S, Blumenthal HJ, Davidson E, Roseman S. Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J Biol Chem 1960; 235: 1265-1273.
17. Norrman J, Myers RB, Giddings TH, Catino EC. Partial Purification of L-glutamine:D-fructose 6-phosphate aminotransferase from zoospores of Blastocladiella emersonii. Biochim Biophys Acta 1973; 302: 173-177.
18. Borgia PT. Roles of the orlA, tsE, and bimG genes of Aspergillus nidulans in chitin synthesis. J Bacteriol 1992; 174: 384-389.
19. Travassos LR. Sporothrix schenckii. In: Szaniszlo PJ, Harris JL (eds). Fungal Dimorphism, with Emphasison Fungi Pathogenic for Humans. New York: Plenum Press, 1985: 121-163.
20. Heller HM, Fuhrer J. Disseminated sporotrichosis in patients with AIDS: case report and review of the literature. AIDS 1991; 5: 1243-1246.
21. Al-Tawfiq JA, Wools KK. Disseminated sporotrichosis and Sporothrix schenckii fungemia as the initial presentation of human immunodeficiency virus infection. Clin Infect Dis 1998; 26: 1403-1406.
22. Durden FM, Elewski B. Fungal infections in HIV-infected patients. Semin Cutan Med Surg 1997; 16: 200-212.
23. Kauffman CA. Sporotrichosis. Clin Infect Dis 1999; 29: 231-236.
24. Gottlieb GS, Lesser CF, Holmes KK, Wald A. Disseminated sporotrichosis associated with treatment with immunosuppressants and tumor necrosis factor-alpha antagonists. Clin Infect Dis 2003; 37: 838-840.
25. Castrejon OV, Robles M, Arroyo OEZ. Fatal fungaemia due to Sporothrix schenckii. Mycoses 1995; 38: 373-376.
26. Lopes-Bezerra LM, Schubach A, Costa RO. Sporothrix schenckii and sporotrichosis. An Acad Bras Cienc 2006; 78: 293-308.
27. Rodriguez del Valle N, Rosario M, Torres Blasini G. Effects of pH, temperature, aeration and carbon source on the development of the mycelial or yeast forms of Sporothrix schenckii from conidia. Mycopathologia 1983; 82: 83-88.
28. Chattaway FW, Holmes MR, Barlow AJ. Cell wall composition of the mycelial and blastospore forms of Candida albicans. J Gen Microbiol 1968; 51: 367-376.
29. Chiew YY, Shepherd MG, Sullivan PA. Regulation of chitin synthesis during germ-tube formation in Candida albicans. Arch Microbiol 1980; 126: 97-104.
30. Shepherd MG, Ghazali HM, Sullivan PA. N-acetyl-D-glucosamine kinase and germ-tube formation in Candida albicans. Exp Mycol 1980; 4: 147-159.
31. Frisa PS, Sonneborn DR. Developmentally regulated interconversions between end product-inhibitable and noninhibitable forms of a first pathway-specific enzyme activity can be mimicked in vitro by protein dephosphorylation-phosphorylation reactions. Proc Nat Acad Sci USA 1982; 79: 6289-6293.
32. Maia JC. Hexosamine and cell wall biogenesis in the aquatic fungus Blastocladiella emersonii. FASEB J 1994; 8: 848-853.
33. Travassos LR, Lloyd KO. Sporothrix schenckii and related species of Ceratocystis. Microbiol Rev 1980; 44: 683-721.
34. Ruiz-Baca E, Toriello C, Perez-Torres A, et al. Isolation and some properties of a glycoprotein of 70 kDa (Gp70) from the cell wall of Sporothrix schenckii involved in fungal adherence to dermal extracellular matrix. Med Mycol 2008; 4: 1-13.
35. Marimon R, Gene J, Cano J, et al. Molecular phylogeny of Sporothrix schenckii. J Clin Microbiol 2006; 44: 3251-3256.
36. Marimon R, Cano J, Gene J, et al. Sporothrix brasiliensis, S. globosa, and S. mexicana, three new Sporothrix species of clinical interest. J Clin Microbiol 2007; 45: 3198-3206.
37. Merril CR. Gel-staining techniques. Meth Enzymol 1990; 182: 477-488.
38. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
39. Ram AF, Arentshorst M, Damveld RA, et al. The cell wall stress response in Aspergillus niger involves increased expression of the glutamine:fructose-6- phosphate amidotransferase-encoding gene ( gfaA ) and increased deposition of chitin in the cell wall. Microbiology 2004; 150: 3315-3326.
40. Dutka-Malen S, Mazodier P, Badet B. Molecular cloning and overexpression of the glucosamine synthetase gene from Escherichia coli. Biochimie 1988; 70: 287-290.
41. McKnight GL, Mudri SL, Mathewes SL, et al. Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase. J Biol Chem 1992; 267: 25208-25212.
42. Milewski S, Gabriel I, Olchowy J. Enzymes of UDP-GlcNAc biosynthesis in yeast. Yeast 2006; 23: 1-14.
43. Miyagi T, Tsuiki S. Comparison of the properties of glucosaminephosphate isomerase (glutamine-forming) from rat liver and a hepatoma. Biochim Biophys Acta 1974; 358: 144-158.
44. Winterburn PJ, Phelps CF. Purification and some kinetic properties of rat liver glucosamine synthetase. Biochem J 1971; 121: 701-709.
45. Ellis DB, Sommar KA. Biosynthesis of respiratory tract mucins. II. Control of hexosamine metabolism by L-glutamine:D-fructose 6-phosphate aminotransferase. Biochim Biophys Acta 1972; 276: 105-112.
46. Watzele G, Tanner W. Cloning of the glutamine:fructose-6-phosphate amidotransferase gene from yeast. Pheromonal regulation of its transcription. J Biol Chem 1989; 264: 8753-8758.
47. Broschat KO, Gorka C, Page JD, et al. Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate. J Biol Chem 2002; 277: 14764-14770.
48. Cifuentes B, Vincente C. Purification and properties of glucosaminephosphate isomerase of Proteus mirabilis. Z Naturforsch [C] 1982; 37: 381-384.
49. Endo A, Kakiki K, Misato T. Feedback inhibition of L-glutamine D-fructose 6-phosphate amidotransferase by uridine diphosphate N-acetylglucosamine in Neurospora crassa. J Bacteriol 1970; 103: 588-594.
50. Vessal M, Hassid WZ. Partial Purification and properties of Lglutamine D-fructose 6-phosphate amidotransferase from Phaseolus aureus. Plant Physiol 1972; 49: 977-981.
51. Kornfeld R. Studies on L-glutamine D-fructose 6-phosphate amidotransferase. I. Feedback inhibition by uridine diphosphate-N- acetylglucosamine. J Biol Chem 1967; 242: 3135-3141
52. Kikuchi H, Tsuiki S. Glucosaminephosphate synthase of human liver. Biochim Biophys Acta 1976; 422: 241-246.
53. Selitrennikoff CP, Dalley NE, Sonneborn DR. Regulation of the hexosamine biosynthetic pathway in the water mold Blastocladiella emersonii: sensitivity to end product inhibition is dependent upon the life cycle phase. Proc Nat Acad Sci USA 1980; 77: 5998-6002
54. Etchebehere LC, Costa Maia MJ. Phosphorylation-dependent regulation of amidotransferase during the development of Blastocladiella emersonii. Arch Biochem Biophys 1989; 272: 301-310.
55. Neuss N, Molloy BB, Shah R, De la Higuera N. The structure of anticapsin, a new biologically active metabolite of Streptomyces griseoplanus . Biochem J 1970; 118: 571-575.
56. Rogers HJ, Newton GGF, Abraham EP. Production and Purification of bacilysin. Biochem J 1965; 97: 573-578.
57. Krynski S, Borowski E, Kuchta A, Borowski J, Becla E. Tetaine, a new antibiotic from Bacillus pumilus strains. Bull State Inst Marine Trop Med 1952; 4: 310-318.
58. Atsumi K, Oiwa R, Omura S. Production of bacillin by Bacillus sp. strain no. KM-208 and its identity with tetaine (bacilysin). J Antibiot 1975; 28: 77-78.
59. Rapp C, Jung G, Katser W, Loeffler W. Chlorotetain from Bacillus subtilis, an antifungal dipeptide with an unusual chlorine-containing amino acid. Angew. Chem Int Ed Engl 1988; 27: 1733-1734.
60. Janiak AM, Hoffmann M, Milewska M, Milewski S. Hydrophobic derivatives of 2-amino-2-deoxy-D-glucitol-6-phosphate: a new type of D-glucosamine-6-phosphate synthase inhibitors with antifungal action. Bioorg Med Chem 2003; 11: 1653-1662.
61. Andruszkiewicz R, Milewski S, Zieniawa T, Borowski E. Anticandidal properties of N3-(4-methoxyfumaroyl)-L-2,3-diaminopropanoic acid oligopeptides. J Med Chem 1990; 33: 132-135.