A fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2-amino- 2-deoxy-α-D-glucopyranoside deacetylase activity

Analytical Biochemistry

Volumn 414, Issue 2, 2011, Pages 278-281

  Huang, Xinyi ^a   Hernick, Marcy ^a  

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

Author keywords

Fluorescamine; Fluorescence; Metal dependent deacetylase; Metallohydrolase; MshB; Mycothiol

Indexed keywords

ACETYLATION; AMINES; DETOXIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

DEACETYLASE; FLUORESCAMINES; METALLOHYDROLASE; MSHB; MYCOTHIOL;

FLUORESCENCE;

ACYLTRANSFERASE; AMIDASE; FLUORESCENT DYE; INOSITOL; MYCOTHIOL; N ACETYL 1 DEXTRO MYO INOSITYL 2 AMINO 2 DEOXY ALPHA DEXTRO GLUCOPYRANOSIDE DEACETYLASE; N ACETYLGLUCOSAMINE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL ANALYSIS; DEACETYLATION; ENZYME ACTIVITY; FLUORESCENCE ANALYSIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; STEADY STATE; STOICHIOMETRY;

EID: 79956083377     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.04.001     Document Type: Article

References (18)

1. G.L. Newton, N. Buchmeier, R.C. Fahey, Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria, Microbiol. Mol. Biol. Rev. 72 (2008) 471-494.
2. V.K. Jothivasan, C.J. Hamilton, Mycothiol: synthesis, biosynthesis, and biological functions of the major low molecular weight thiol in actinomycetes, Nat. Prod. Rep. 25 (2008) 1091-1117.
3. M. Rawat, Y. Av-Gay, Mycothiol-dependent proteins in actinomycetes, FEMS Microbiol. Rev. 31 (2007) 278-292.
4. F. Fan, M.W. Vetting, P.A. Frantom, J.S. Blanchard, Structures and mechanisms of the mycothiol biosynthetic enzymes, Curr. Opin. Chem. Biol. 13 (2009) 451-459.
5. M.-T. Gutierrez-Lugo, H. Baker, J. Shiloach, H. Boshoff, C.A. Bewley, Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening, J. Biomol. Screen. 14 (2009) 643-652.
6. D.W. Gammon, D.J. Steenkamp, V. Mavumengwana, M.J. Marakalala, T.T. Mudzunga, R. Hunter, M. Munyololo, Conjugates of plumbagin and phenyl-2- amino-1-thioglucoside inhibit MshB, a deacetylase involved in the biosynthesis of mycothiol, Bioorg. Med. Chem. 18 (2010) 2501-2514.
7. M.-T. Gutierrez-Lugo, C.A. Bewley, Natural products, small molecules, and genetics in tuberculosis drug development, J. Med. Chem. 51 (2008) 2606-2612. (Pubitemid 351620780)
8. B.B. Metaferia, B.J. Fetterolf, S. Shazad-ul-Hussan, M. Moravec, J.A. Smith, S. Ray, M.-T. Gutierrez-Lugo, C.A. Bewley, Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol-associated enzymes: the first inhibitors of GlcNAc - Ins deacetylase, J. Med. Chem. 50 (2007) 6326-6336.
9. G.M. Nicholas, L.L. Eckman, G.L. Newton, R.C. Fahey, S. Ray, C.A. Bewley, Inhibition and kinetics of Mycobacterium tuberculosis and Mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors, Bioorg. Med. Chem. 11 (2003) 601-608. (Pubitemid 36132237)
10. D.P. Bhave, W.B.I. Muse, K.S. Carroll, Drug targets in mycobacterial sulfur metabolism, Infect. Disord. Drug Targets 7 (2007) 140-158.
11. G.L. Newton, Y. Av-Gay, R.C. Fahey, N-Acetyl-1-D-myo-inosityl-2-amino-2- deoxy-a-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis, J. Bacteriol. 182 (2000) 6958-6963.
12. G.L. Newton, M. Ko, P. Ta, Y. Av-Gay, R.C. Fahey, Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2- acetamido-2-deoxy-a-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme, Protein Expr. Purif. 47 (2006) 542-550. (Pubitemid 43729027)
13. S.J. Anderberg, G.L. Newton, R.C. Fahey, Mycothiol biosynthesis and metabolism: cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in Mycobacterium smegmatis, J. Biol. Chem. 273 (1998) 30391-30397.
14. G.M. Nicholas, L.L. Eckman, P. Kovac, S. Otero-Quintero, C.A. Bewley, Synthesis of 1-D- and 1-l-myo-inosityl 2-N-acetamido-2-deoxy- α-D-glucopyranoside establishes substrate specificity of the Mycobacterium tuberculosis enzyme AcGI deacetylase, Bioorg. Med. Chem. 11 (2003) 2641-2647. (Pubitemid 36566625)
15. W. Wang, M. Maniar, R. Jain, J. Jacobs, J. Trias, Z.Y. Yuan, A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3- hydroxymyristoyl)-N-acetylglucosamine deacetylase, Anal. Biochem. 290 (2001) 338-346.
16. M.C. Pirrung, L.N. Tumey, C.R. Raetz, J.E. Jackman, K. Snehalatha, A.L. McClerren, C.A. Fierke, S.L. Gantt, K.M. Rusche, Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): isoxazoline zinc amidase inhibitors bearing diverse metal binding groups, J. Med. Chem. 45 (2002) 4359-4370.
17. P. Sobrado, M.A. Goren, D. James, C.K. Amundson, B.G. Fox, A protein structure initiative approach to expression, purification, and in situ delivery of human cytochrome b5 to membrane vesicles, Protein Expr. Purif. 58 (2008) 229-241.
18. M. Steffek, G.L. Newton, Y. Av-Gay, R.C. Fahey, Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase, Biochemistry 42 (2003) 12067-12076. (Pubitemid 37280657)