메뉴 건너뛰기




Volumn 22, Issue 2, 2013, Pages 222-230

Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity

Author keywords

Acetylation of antibiotics; Broadsubstrate screen; Ellman's reagent; Gcn5 related acetyltransferase; GNAT; N acetyltransferase

Indexed keywords

ACYLTRANSFERASE; ADENOSINE; ALLANTOIN; AMINONUCLEOSIDE; AMPICILLIN; APRAMYCIN; BACITRACIN; CATECHOLAMINE; CEFALEXIN; CEPHALOSPORIN; CHLORAMPHENICOL; COLISTIN; CYSTEINE; CYTIDINE; FOLIC ACID; GENERAL CONTROL OF NUTRITION RELATED N ACETYLTRANSFERASE; GUANOSINE; KANAMYCIN B; POLYAMINE; POLYMYXIN B; PUROMYCIN; PYRIDOXAMINE; STREPTOMYCIN; SULFACETAMIDE; SULFONAMIDE; THIAMINE; TOBRAMYCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; UREA; VITAMIN;

EID: 84874049400     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2199     Document Type: Article
Times cited : (46)

References (37)
  • 3
    • 0030954208 scopus 로고    scopus 로고
    • Gcn5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald AF, Landsman D (1997) Gcn5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem Sci 22:154-155.
    • (1997) Trends Biochem Sci , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 4
    • 33845292279 scopus 로고    scopus 로고
    • Activity-based substrate profiling for Gcn5-related N-acetyltransferases: The use of chloroacetyl-coenzyme A to identify protein substrates
    • Yu M, de Carvalho LPS, Sun G, Blanchard JS (2006) Activity-based substrate profiling for Gcn5-related N-acetyltransferases: The use of chloroacetyl-coenzyme A to identify protein substrates. J Am Chem Soc 128: 15356-15357.
    • (2006) J Am Chem Soc , vol.128 , pp. 15356-15357
    • Yu, M.1    De Carvalho, L.P.S.2    Sun, G.3    Blanchard, J.S.4
  • 5
    • 1942490112 scopus 로고    scopus 로고
    • A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
    • Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS (2004) A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chem Biol 11:565-573.
    • (2004) Chem Biol , vol.11 , pp. 565-573
    • Vetting, M.W.1    Magnet, S.2    Nieves, E.3    Roderick, S.L.4    Blanchard, J.S.5
  • 7
    • 1042300238 scopus 로고    scopus 로고
    • Biochemical and structural characterization of recombinant histone acetyltransferase proteins
    • Allis CD, Carl W, Eds. . Academic Press, New York
    • Ronen M, Biochemical and structural characterization of recombinant histone acetyltransferase proteins. In: Allis CD, Carl W, Eds. (2003) Methods in Enzymology. Academic Press, New York, pp 106-119.
    • (2003) Methods in Enzymology , pp. 106-119
    • Ronen, M.1
  • 8
    • 0033135707 scopus 로고    scopus 로고
    • Crystal structure of an aminoglycoside 60-Nacetyltransferase: Defining the Gcn5-related N-acetyltransferase superfamily fold
    • Wybenga-Groot LE, Draker K-A, Wright GD, Berghuis AM (1999) Crystal structure of an aminoglycoside 60-Nacetyltransferase: Defining the Gcn5-related N-acetyltransferase superfamily fold. Structure 7:497-507.
    • (1999) Structure , vol.7 , pp. 497-507
    • Wybenga-Groot, L.E.1    Draker, K.-A.2    Wright, G.D.3    Berghuis, A.M.4
  • 9
    • 77957234949 scopus 로고    scopus 로고
    • A high-throughput colorimetric assay to characterize the enzyme kinetic and cellular activity of spermidine/spermine N1-acetyltransferase
    • Lin H-J, Lien Y-C, Hsu C-H (2010) A high-throughput colorimetric assay to characterize the enzyme kinetic and cellular activity of spermidine/spermine N1-acetyltransferase Anal Biochem 407:226-232.
    • (2010) Anal Biochem , vol.407 , pp. 226-232
    • Lin, H.-J.1    Lien, Y.-C.2    Hsu, C.-H.3
  • 11
    • 82455162549 scopus 로고    scopus 로고
    • Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU
    • Zhou Y, Xin Y, Sha S, Ma Y (2011) Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU. Arch Microbiol 193:751-757.
    • (2011) Arch Microbiol , vol.193 , pp. 751-757
    • Zhou, Y.1    Xin, Y.2    Sha, S.3    Ma, Y.4
  • 12
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • George L E (1958) A colorimetric method for determining low concentrations of mercaptans. Arch Biochem Biophys 74:443-450.
    • (1958) Arch Biochem Biophys , vol.74 , pp. 443-450
    • George, L.E.1
  • 13
    • 0009761277 scopus 로고
    • Alkaline decomposition of organic disulfides. IV. Limitation on the use of Ellman's reagent 2,20-dinitro-5,50-dithiodibenzoic acid
    • Danehy JP, Elia VJ, Lavelle CJ (1971) Alkaline decomposition of organic disulfides. IV. Limitation on the use of Ellman's reagent. 2,20-dinitro-5,50- dithiodibenzoic acid. J Org Chem 36:1003-1005.
    • (1971) J Org Chem , vol.36 , pp. 1003-1005
    • Danehy, J.P.1    Elia, V.J.2    Lavelle, C.J.3
  • 14
    • 78751554991 scopus 로고    scopus 로고
    • Chemical approaches for the detection and synthesis of acetylated proteins
    • Yang Y-Y, Hang HC (2011) Chemical approaches for the detection and synthesis of acetylated proteins. Chem-BioChem 12:314-322.
    • (2011) Chem-BioChem , vol.12 , pp. 314-322
    • Yang, Y.-Y.1    Hang, H.C.2
  • 15
    • 0033532182 scopus 로고    scopus 로고
    • Yeast methionine aminopeptidase i
    • Walker KW, Bradshaw RA (1999) Yeast methionine aminopeptidase I. J Biol Chem 274:13403-13409.
    • (1999) J Biol Chem , vol.274 , pp. 13403-13409
    • Walker, K.W.1    Bradshaw, R.A.2
  • 16
    • 84856619953 scopus 로고    scopus 로고
    • Repeated isolation of Pseudomonas aeruginosa isolates resistant to both polymyxins and carbapenems from one patient
    • Lee J-Y, Lim MH, Heo ST, Ko KS (2012) Repeated isolation of Pseudomonas aeruginosa isolates resistant to both polymyxins and carbapenems from one patient. Diagn Microbiol Infect Dis 72:267-271.
    • (2012) Diagn Microbiol Infect Dis , vol.72 , pp. 267-271
    • Lee, J.-Y.1    Lim, M.H.2    Heo, S.T.3    Ko, K.S.4
  • 17
    • 77955376940 scopus 로고    scopus 로고
    • Adaptive resistance to the ''last hope'' antibiotics polymyxin B and colistin in Pseudomonas aeruginosa is mediated by the novel twocomponent regulatory system ParR-ParS
    • Fernandez L, Gooderham WJ, Bains M, McPhee JB, Wiegand I, Hancock REW (2010) Adaptive resistance to the ''last hope'' antibiotics polymyxin B and colistin in Pseudomonas aeruginosa is mediated by the novel twocomponent regulatory system ParR-ParS. Antimicrob Agents Chemother 54:3372-3382.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 3372-3382
    • Fernandez, L.1    Gooderham, W.J.2    Bains, M.3    McPhee, J.B.4    Wiegand, I.5    Hancock, R.E.W.6
  • 18
    • 77950650563 scopus 로고    scopus 로고
    • Polymyxin B resistance in El Tor Vibrio cholerae requires lipid acylation catalyzed by MsbB
    • Matson JS, Yoo HJ, Hakansson K, DiRita VJ (2010) Polymyxin B resistance in El Tor Vibrio cholerae requires lipid acylation catalyzed by MsbB. J Bacteriol 192:2044-2052.
    • (2010) J Bacteriol , vol.192 , pp. 2044-2052
    • Matson, J.S.1    Yoo, H.J.2    Hakansson, K.3    Dirita, V.J.4
  • 19
    • 0022336717 scopus 로고
    • Biosynthesis of puromycin by Streptomyces alboniger: Characterization of puromycin N-acetyltransferase
    • Vara J, Perez-Gonzalez JA, Jimenez A (1985) Biosynthesis of puromycin by Streptomyces alboniger: Characterization of puromycin N-acetyltransferase. Biochemis try 24:8074-8081.
    • (1985) Biochemis Try , vol.24 , pp. 8074-8081
    • Vara, J.1    Perez-Gonzalez, J.A.2    Jimenez, A.3
  • 21
    • 79960440908 scopus 로고    scopus 로고
    • In: Lyte M, Freestone PPE, Eds. Microbial endocrinology: Interkingdom signaling in infectious disease and health. New York: Springer
    • Roshchina VV, Evolutionary considerations of neurotransmitters in microbial, plant, and animal cells. In: Lyte M, Freestone PPE, Eds. (2010) Microbial endocrinology: Interkingdom signaling in infectious disease and health. New York: Springer, pp 17-52.
    • (2010) Evolutionary Considerations of Neurotransmitters in Microbial, Plant, and Animal Cells , pp. 17-52
    • Roshchina, V.V.1
  • 23
    • 35248895963 scopus 로고    scopus 로고
    • Animal neurotransmitter substances in plants
    • Odjakova M, Hadjivanova C (1997) Animal neurotransmitter substances in plants. Bulg J Plant Physiol 23: 94-102.
    • (1997) Bulg J Plant Physiol , vol.23 , pp. 94-102
    • Odjakova, M.1    Hadjivanova, C.2
  • 24
    • 34547539768 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase
    • Zhao P, Li J, Wang Y, Jiang H (2007) Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase. Insect Biochem Mol Biol 37:952-959.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 952-959
    • Zhao, P.1    Li, J.2    Wang, Y.3    Jiang, H.4
  • 25
    • 13644260621 scopus 로고    scopus 로고
    • Overexpression and characterization of an aminoglycoside 60-N-acetyltransferase with broad specificity from an e-poly-L-lysine producer, Streptomyces albulus IFO 14147
    • Hamano Y, Hoshino Y, Nakamori S, Takagi H (2004) Overexpression and characterization of an aminoglycoside 60-N-acetyltransferase with broad specificity from an e-poly-L-lysine producer, Streptomyces albulus IFO 14147. J Biochem 136:517-524.
    • (2004) J Biochem , vol.136 , pp. 517-524
    • Hamano, Y.1    Hoshino, Y.2    Nakamori, S.3    Takagi, H.4
  • 26
    • 0036707544 scopus 로고    scopus 로고
    • Aminoglycoside 20-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates
    • Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL (2002) Aminoglycoside 20-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat Struct Mol Biol 9:653-658.
    • (2002) Nat Struct Mol Biol , vol.9 , pp. 653-658
    • Vetting, M.W.1    Hegde, S.S.2    Javid-Majd, F.3    Blanchard, J.S.4    Roderick, S.L.5
  • 27
    • 77954913118 scopus 로고    scopus 로고
    • Codominant expression of N-acetylation and O-acetylation activities catalyzed by N-acetyltransferase 2 in human hepatocytes
    • Doll MA, Zang Y, Moeller T, Hein DW (2010) Codominant expression of N-acetylation and O-acetylation activities catalyzed by N-acetyltransferase 2 in human hepatocytes. J Pharmacol Exp Ther 334:540-544.
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 540-544
    • Doll, M.A.1    Zang, Y.2    Moeller, T.3    Hein, D.W.4
  • 28
    • 33749018560 scopus 로고    scopus 로고
    • Insights into the O-acetylation reaction of hydroxylated heterocyclic amines by human arylamine N-acetyltransferases: A computational study
    • Lau EY, Felton JS, Lightstone FC (2006) Insights into the O-acetylation reaction of hydroxylated heterocyclic amines by human arylamine N-acetyltransferases: A computational study. Chem Res Toxicol 19:1182-1190.
    • (2006) Chem Res Toxicol , vol.19 , pp. 1182-1190
    • Lau, E.Y.1    Felton, J.S.2    Lightstone, F.C.3
  • 30
    • 79960083570 scopus 로고    scopus 로고
    • Crystal structure of the novel PaiA N-acetyltransferase from thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production
    • Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF (2011) Crystal structure of the novel PaiA N-acetyltransferase from thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production. Proteins 79: 2566-2577.
    • (2011) Proteins , vol.79 , pp. 2566-2577
    • Filippova, E.V.1    Shuvalova, L.2    Minasov, G.3    Kiryukhina, O.4    Zhang, Y.5    Clancy, S.6    Radhakrishnan, I.7    Joachimiak, A.8    Anderson, W.F.9
  • 32
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols L, Gu M, Dieckman L, Raffen R, Collart FR, Donnelly MI (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Express Purif 25: 8-15.
    • (2002) Protein Express Purif , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 33
    • 0037790957 scopus 로고    scopus 로고
    • A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles
    • Sanville Millard C, Stols L, Quartey P, Kim Y, Dementieva I, Donnelly MI (2003) A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles. Protein Express Purif 29:311-320.
    • (2003) Protein Express Purif , vol.29 , pp. 311-320
    • Sanville Millard, C.1    Stols, L.2    Quartey, P.3    Kim, Y.4    Dementieva, I.5    Donnelly, M.I.6
  • 34
    • 0033939135 scopus 로고    scopus 로고
    • Controlled intracellular processing of fusion proteins by TEV protease
    • Kapust RB, Waugh DS (2000) Controlled intracellular processing of fusion proteins by TEV protease. Protein Express Purif 19:312-318.
    • (2000) Protein Express Purif , vol.19 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 35
    • 34447500591 scopus 로고    scopus 로고
    • Kinetic and structural analysis of the early oxidation products of dopamine
    • Bisaglia M, Mammi S, Bubacco L (2007) Kinetic and structural analysis of the early oxidation products of dopamine. J Biol Chem 282:15597-15605.
    • (2007) J Biol Chem , vol.282 , pp. 15597-15605
    • Bisaglia, M.1    Mammi, S.2    Bubacco, L.3
  • 36
    • 0020799596 scopus 로고
    • Mechanism of the oxidation of dopamine by the hydroxyl radical in aqueous solution
    • Richter HW, Waddell WH (1983) Mechanism of the oxidation of dopamine by the hydroxyl radical in aqueous solution. J Am Chem Soc 105:5434-5440.
    • (1983) J Am Chem Soc , vol.105 , pp. 5434-5440
    • Richter, H.W.1    Waddell, W.H.2
  • 37
    • 0031900371 scopus 로고    scopus 로고
    • Diphenol oxidases, enzyme-catalysed browning and plant disease resistance
    • Walker JRL, Ferrar PH (1998) Diphenol oxidases, enzyme-catalysed browning and plant disease resistance. Biotechnol Genet Eng Rev 15:457-498.
    • (1998) Biotechnol Genet Eng Rev , vol.15 , pp. 457-498
    • Walker, J.R.L.1    Ferrar, P.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.