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Volumn 287, Issue 13, 2012, Pages 10424-10434

Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy- α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosine

Author keywords

[No Author keywords available]

Indexed keywords

ACID BASE; ACID CATALYST; CATALYTIC MECHANISMS; CHEMICAL MECHANISM; DEACETYLASE; DRUG DEVELOPMENT; GENERAL BASE; GLUTATHIONES; GRAM-POSITIVE BACTERIUM; MUTAGENESIS EXPERIMENT; MYCOBACTERIAL; MYCOBACTERIUM TUBERCULOSIS; OXYANIONS; PRODUCT RELEASE; REACTIVE NUCLEOPHILES; SIDE-CHAINS; SMALL MOLECULES; SUBSTRATE BINDING;

EID: 84858972822     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.320184     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 51949098757 scopus 로고    scopus 로고
    • Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria
    • Newton, G. L., Buchmeier, N., and Fahey, R. C. (2008) Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria. Microbiol. Mol. Biol. Rev. 72, 471-494
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 471-494
    • Newton, G.L.1    Buchmeier, N.2    Fahey, R.C.3
  • 2
    • 58949091991 scopus 로고    scopus 로고
    • Mycothiol. Synthesis, biosynthesis, and biological functions of the major low molecular weight thiol in actinomycetes
    • Jothivasan, V. K., and Hamilton, C. J. (2008) Mycothiol. Synthesis, biosynthesis, and biological functions of the major low molecular weight thiol in actinomycetes. Nat. Prod. Rep. 25, 1091-1117
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 1091-1117
    • Jothivasan, V.K.1    Hamilton, C.J.2
  • 3
    • 34047223584 scopus 로고    scopus 로고
    • Mycothiol-dependent proteins in actinomycetes
    • DOI 10.1111/j.1574-6976.2006.00062.x
    • Rawat, M., and Av-Gay, Y. (2007) Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol. Rev. 31, 278-292 (Pubitemid 46540312)
    • (2007) FEMS Microbiology Reviews , vol.31 , Issue.3 , pp. 278-292
    • Rawat, M.1    Av-Gay, Y.2
  • 5
    • 77950041558 scopus 로고    scopus 로고
    • Conjugates of plumbagin and phenyl-2-amino-1-thioglucoside inhibit MshB, a deacetylase involved in the biosynthesis of mycothiol
    • Gammon, D. W., Steenkamp, D. J., Mavumengwana, V., Marakalala, M. J., Mudzunga, T. T., Hunter, R., and Munyololo, M. (2010) Conjugates of plumbagin and phenyl-2-amino-1-thioglucoside inhibit MshB, a deacetylase involved in the biosynthesis of mycothiol. Bioorg. Med. Chem. 18, 2501-2514
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2501-2514
    • Gammon, D.W.1    Steenkamp, D.J.2    Mavumengwana, V.3    Marakalala, M.J.4    Mudzunga, T.T.5    Hunter, R.6    Munyololo, M.7
  • 6
    • 67651064692 scopus 로고    scopus 로고
    • Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening
    • Gutierrez-Lugo, M. T., Baker, H., Shiloach, J., Boshoff, H., and Bewley, C. A. (2009) Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening. J. Biomol. Screen. 14, 643-652
    • (2009) J. Biomol. Screen. , vol.14 , pp. 643-652
    • Gutierrez-Lugo, M.T.1    Baker, H.2    Shiloach, J.3    Boshoff, H.4    Bewley, C.A.5
  • 7
    • 42949174608 scopus 로고    scopus 로고
    • Natural products, small molecules, and genetics in tuberculosis drug development
    • Gutierrez-Lugo, M. T., and Bewley, C. A. (2008) Natural products, small molecules, and genetics in tuberculosis drug development. J. Med. Chem. 51, 2606-2612
    • (2008) J. Med. Chem. , vol.51 , pp. 2606-2612
    • Gutierrez-Lugo, M.T.1    Bewley, C.A.2
  • 8
    • 37049001071 scopus 로고    scopus 로고
    • Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol-associated enzymes: The first inhibitors of GlcNAc-Ins deacetylase
    • DOI 10.1021/jm070669h
    • Metaferia, B. B., Fetterolf, B. J., Shazad-Ul-Hussan, S., Moravec, M., Smith, J. A., Ray, S., Gutierrez-Lugo, M. T., and Bewley, C. A. (2007) Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol- associated enzymes. The first inhibitors of GlcNAc-Ins deacetylase. J. Med. Chem. 50, 6326-6336 (Pubitemid 350250420)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.25 , pp. 6326-6336
    • Metaferia, B.B.1    Fetterolf, B.J.2    Shazad-ul-Hussan, S.3    Moravec, M.4    Smith, J.A.5    Ray, S.6    Gutierrez-Lugo, M.-T.7    Bewley, C.A.8
  • 9
    • 0037245381 scopus 로고    scopus 로고
    • Inhibition and kinetics of mycobacterium tuberculosis and Mycobacterium Smegmatis mycothiol-S-conjugate amidase by natural product inhibitors
    • DOI 10.1016/S0968-0896(02)00345-0, PII S0968089602003450
    • Nicholas, G. M., Eckman, L. L., Newton, G. L., Fahey, R. C., Ray, S., and Bewley, C. A. (2003) Inhibition and kinetics of mycobacterium tuberculosis and mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors. Bioorg. Med. Chem. 11, 601-608 (Pubitemid 36132237)
    • (2003) Bioorganic and Medicinal Chemistry , vol.11 , Issue.4 , pp. 601-608
    • Nicholas, G.M.1    Eckman, L.L.2    Newton, G.L.3    Fahey, R.C.4    Ray, S.5    Bewley, C.A.6
  • 11
    • 0034460953 scopus 로고    scopus 로고
    • N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis
    • DOI 10.1128/JB.182.24.6958-6963.2000
    • Newton, G. L., Av-Gay, Y., and Fahey, R. C. (2000) N-Acetyl-1-D-myo- inosityl- 2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182, 6958-6963 (Pubitemid 32259599)
    • (2000) Journal of Bacteriology , vol.182 , Issue.24 , pp. 6958-6963
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 12
    • 33646546739 scopus 로고    scopus 로고
    • Purification and characterization of Mycobacterium tuberculosis 1d-myo-inosityl-2-acetamido-2-deoxy-α-d-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme
    • DOI 10.1016/j.pep.2006.03.003, PII S1046592806000775
    • Newton, G. L., Ko, M., Ta, P., Av-Gay, Y., and Fahey, R. C. (2006) Purification and characterization of Mycobacterium tuberculosis 1-D-myo-Inosityl- 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme. Protein Expr. Purif. 47, 542-550 (Pubitemid 43729027)
    • (2006) Protein Expression and Purification , vol.47 , Issue.2 , pp. 542-550
    • Newton, G.L.1    Ko, M.2    Ta, P.3    Av-Gay, Y.4    Fahey, R.C.5
  • 13
    • 0038673392 scopus 로고    scopus 로고
    • 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
    • DOI 10.1016/S0968-0896(03)00154-8
    • Nicholas, G. M., Eckman, L. L., Kovác, P., Otero-Quintero, S., and Bewley, C. A. (2003) 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, 2641-2647 (Pubitemid 36566625)
    • (2003) Bioorganic and Medicinal Chemistry , vol.11 , Issue.12 , pp. 2641-2647
    • Nicholas, G.M.1    Eckman, L.L.2    Kovac, P.3    Otero-Quintero, S.4    Bewley, C.A.5
  • 14
    • 79957983435 scopus 로고    scopus 로고
    • The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2- amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions
    • Huang, X., Kocabas, E., and Hernick, M. (2011) The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D- glucopyranoside deacetylase (MshB) change depending on environmental conditions. J. Biol. Chem. 286, 20275-20282
    • (2011) J. Biol. Chem. , vol.286 , pp. 20275-20282
    • Huang, X.1    Kocabas, E.2    Hernick, M.3
  • 15
    • 0345306583 scopus 로고    scopus 로고
    • The Crystal Structure of 1-D-myo-Inosityl 2-Acetamido-2-deoxy-α -D-glucopyranoside Deacetylase (MshB) from Mycobacterium tuberculosis Reveals a Zinc Hydrolase with a Lactate Dehydrogenase Fold
    • DOI 10.1074/jbc.M308914200
    • Maynes, J. T., Garen, C., Cherney, M. M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R. C., and James, M. N. (2003) The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278, 47166-47170 (Pubitemid 37452303)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47166-47170
    • Maynes, J.T.1    Garen, C.2    Cherney, M.M.3    Newton, G.4    Arad, D.5    Av-Gay, Y.6    Fahey, R.C.7    James, M.N.G.8
  • 16
    • 0346493029 scopus 로고    scopus 로고
    • Crystal Structure of MshB from Mycobacterium tuberculosis, a Deacetylase Involved in Mycothiol Biosynthesis
    • DOI 10.1016/j.jmb.2003.11.034
    • McCarthy, A. A., Peterson, N. A., Knijff, R., and Baker, E. N. (2004) Crystal structure of MshB from Mycobacterium tuberculosis, a deacetylase involved in mycothiol biosynthesis. J. Mol. Biol. 335, 1131-1141 (Pubitemid 38091615)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 1131-1141
    • McCarthy, A.A.1    Peterson, N.A.2    Knijff, R.3    Baker, E.N.4
  • 17
    • 77954218410 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors
    • Supuran, C. T. (2010) Carbonic anhydrase inhibitors. Bioorg. Med. Chem. Lett. 20, 3467-3474
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 3467-3474
    • Supuran, C.T.1
  • 18
  • 19
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag, M., and Salvesen, G. S. (2010) Emerging principles in protease-based drug discovery. Nat. Rev. Drug Discov. 9, 690-701
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 20
    • 0141535260 scopus 로고    scopus 로고
    • Targeting metalloenzymes: A strategy that works
    • DOI 10.1016/S1471-4892(03)00115-2, PII S1471489203001152
    • White, R. J., Margolis, P. S., Trias, J., and Yuan, Z. (2003) Targeting metalloenzymes. A strategy that works. Curr. Opin. Pharmacol. 3, 502-507 (Pubitemid 37221130)
    • (2003) Current Opinion in Pharmacology , vol.3 , Issue.5 , pp. 502-507
    • White, R.J.1    Margolis, P.S.2    Trias, J.3    Yuan, Z.4
  • 21
    • 77958584265 scopus 로고    scopus 로고
    • Mechanisms of metal-dependent hydrolases in metabolism
    • Mander, L. N., and Lui, H.-W. B., eds Elsevier Science Publishing Co., Inc., New York
    • Hernick, M., and Fierke, C. A. (2010) Mechanisms of metal-dependent hydrolases in metabolism. in Comprehensive Natural Products II (Mander, L. N., and Lui, H.-W. B., eds) pp. 547-581, Elsevier Science Publishing Co., Inc., New York
    • (2010) Comprehensive Natural Products II , pp. 547-581
    • Hernick, M.1    Fierke, C.A.2
  • 23
    • 79956083377 scopus 로고    scopus 로고
    • A fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2- amino-2-deoxy-α-D-glucopyranoside deacetylase activity
    • Huang, X., and Hernick, M. (2011) A fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase activity. Anal. Biochem. 414, 278-281
    • (2011) Anal. Biochem. , vol.414 , pp. 278-281
    • Huang, X.1    Hernick, M.2
  • 24
    • 34447310567 scopus 로고    scopus 로고
    • N-acetyl-D-glucosamine-6-phosphate deacetylase: Substrate activation via a single divalent metal ion
    • DOI 10.1021/bi700543x
    • Hall, R. S., Xiang, D. F., Xu, C., and Raushel, F. M. (2007) N-Acetyl-D-glucosamine- 6-phosphate deacetylase. Substrate activation via a single divalent metal ion. Biochemistry 46, 7942-7952 (Pubitemid 47051630)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 7942-7952
    • Hall, R.S.1    Dao, F.X.2    Xu, C.3    Raushel, F.M.4
  • 25
    • 58649114732 scopus 로고    scopus 로고
    • Dissection of the stepwise mechanism to β-lactam formation and elucidation of a rate-determining conformational change in β-lactam synthetase
    • Raber, M. L., Freeman, M. F., and Townsend, C. A. (2009) Dissection of the stepwise mechanism to β-lactam formation and elucidation of a rate-determining conformational change in β-lactam synthetase. J. Biol. Chem. 284, 207-217
    • (2009) J. Biol. Chem. , vol.284 , pp. 207-217
    • Raber, M.L.1    Freeman, M.F.2    Townsend, C.A.3
  • 28
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack, R. L. (2002) Rotamer libraries in the 21st century. Curr. Opin. Struct. Biol. 12, 431-440
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack, R.L.1
  • 29
    • 34547863927 scopus 로고    scopus 로고
    • Rate-limiting steps and role of active site lys443 in the mechanism of carbapenam synthetase
    • DOI 10.1021/bi0618464
    • Arnett, S. O., Gerratana, B., and Townsend, C. A. (2007) Rate-limiting steps and role of active site Lys-443 in the mechanism of carbapenam synthetase. Biochemistry 46, 9337-9345 (Pubitemid 47255046)
    • (2007) Biochemistry , vol.46 , Issue.32 , pp. 9337-9345
    • Arnett, S.O.1    Gerratana, B.2    Townsend, C.A.3
  • 30
    • 0030018850 scopus 로고    scopus 로고
    • Structural flexibility modulates the activity of human glutathione transferase P1-1: Role of helix 2 flexibility in the catalytic mechanism
    • DOI 10.1074/jbc.271.27.16187
    • Ricci, G., Caccuri, A. M., Lo Bello, M., Rosato, N., Mei, G., Nicotra, M., Chiessi, E., Mazzetti, A. P., and Federici, G. (1996) Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism. J. Biol. Chem. 271, 16187-16192 (Pubitemid 26236236)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.27 , pp. 16187-16192
    • Ricci, G.1    Caccuri, A.M.2    Bello, M.L.3    Rosato, N.4    Mei, G.5    Nicotra, M.6    Chiessi, E.7    Mazzetti, A.P.8    Federici, G.9
  • 31
    • 66649135261 scopus 로고    scopus 로고
    • A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes. Carbapenam synthetase and β-lactam synthetase
    • Raber, M. L., Arnett, S. O., and Townsend, C. A. (2009) A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes. Carbapenam synthetase and β-lactam synthetase. Biochemistry 48, 4959-4971
    • (2009) Biochemistry , vol.48 , pp. 4959-4971
    • Raber, M.L.1    Arnett, S.O.2    Townsend, C.A.3
  • 32
    • 0030950429 scopus 로고    scopus 로고
    • Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: A two-metal ion mechanism for peptide hydrolysis
    • DOI 10.1021/bi9618676
    • Chen, G., Edwards, T., D'souza, V. M., and Holz, R. C. (1997) Mechanistic studies on the aminopeptidase from Aeromonas proteolytica. A two-metal ion mechanism for peptide hydrolysis. Biochemistry 36, 4278-4286 (Pubitemid 27171601)
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4278-4286
    • Chen, G.1    Edwards, T.2    D'Souza, V.M.3    Holz, R.C.4
  • 33
    • 0034673105 scopus 로고    scopus 로고
    • Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase
    • DOI 10.1021/bi992177f
    • Javid-Majd, F., and Blanchard, J. S. (2000) Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase. Biochemistry 39, 1285-1293 (Pubitemid 30090696)
    • (2000) Biochemistry , vol.39 , Issue.6 , pp. 1285-1293
    • Javid-Majd, F.1    Blanchard, J.S.2
  • 34
    • 0034625058 scopus 로고    scopus 로고
    • Fluoride inhibition of Klebsiella aerogenes urease: Mechanistic implications of a pseudo-uncompetitive, slow-binding inhibitor
    • DOI 10.1021/bi992287m
    • Todd, M. J., and Hausinger, R. P. (2000) Fluoride inhibition of Klebsiella aerogenes urease. mechanistic implications of a pseudo-uncompetitive, slow-binding inhibitor. Biochemistry 39, 5389-5396 (Pubitemid 30257079)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5389-5396
    • Todd, M.J.1    Hausinger, R.P.2
  • 35
    • 0032813321 scopus 로고    scopus 로고
    • Different phosphate binding modes of Streptomyces griseus aminopeptidase between crystal and solution states and the status of zinc-bound water
    • DOI 10.1016/S0014-5793(99)00879-0, PII S0014579399008790
    • Harris, M. N., and Ming, L. J. (1999) Different phosphate binding modes of Streptomyces griseus aminopeptidase between crystal and solution states and the status of zinc-bound water. FEBS Lett. 455, 321-324 (Pubitemid 29333060)
    • (1999) FEBS Letters , vol.455 , Issue.3 , pp. 321-324
    • Harris, M.N.1    Ming, L.-J.2
  • 36
    • 0020346954 scopus 로고
    • Solvent isotope effects of enzyme systems
    • Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects of enzyme systems. Methods Enzymol. 87, 551-606
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 37
    • 20444469255 scopus 로고    scopus 로고
    • UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism
    • DOI 10.1074/jbc.M413560200
    • Hernick, M., Gennadios, H. A., Whittington, D. A., Rusche, K. M., Christianson, D. W., and Fierke, C. A. (2005) UDP-3-O-((R)-3-hydroxymyristoyl)- N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280, 16969-16978 (Pubitemid 41389158)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16969-16978
    • Hernick, M.1    Gennadios, H.A.2    Whittington, D.A.3    Rusche, K.M.4    Christianson, D.W.5    Fierke, C.A.6
  • 38
    • 0031439461 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    • DOI 10.1021/bi972223g
    • Cha, J., and Auld, D. S. (1997) Site-directed mutagenesis of the active site glutamate in human matrilysin. Investigation of its role in catalysis. Biochemistry 36, 16019-16024 (Pubitemid 28027407)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 16019-16024
    • Cha, J.1    Auld, D.S.2


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