메뉴 건너뛰기




Volumn 64, Issue 2, 2012, Pages 164-172

Site-directed mutagenesis studies on the l-arginine-binding sites of feedback inhibition in N-acetyl-l-glutamate kinase (NAGK) from corynebacterium glutamicum

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUTAMATE KINASE; ARGININE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84856951326     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-011-0042-y     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 55549146817 scopus 로고    scopus 로고
    • Nitrate-responsive NarX-NarL represses arginine-mediated induction of the Pseudomonas aeruginosa arginine fermentation arcDABC operon
    • 10.1099/mic.0.2008/018929-0 10.1099/mic.0.2008/018929-0 1:CAS:528:DC%2BD1cXhtlagtbjN
    • B Benkert N Quack K Schreiber L Jaensch D Jahn M Schobert 2008 Nitrate-responsive NarX-NarL represses arginine-mediated induction of the Pseudomonas aeruginosa arginine fermentation arcDABC operon Microbiol SGM 154 3053 3060 10.1099/mic.0.2008/018929-0 10.1099/mic.0.2008/018929-0 1:CAS:528:DC%2BD1cXhtlagtbjN
    • (2008) Microbiol SGM , vol.154 , pp. 3053-3060
    • Benkert, B.1    Quack, N.2    Schreiber, K.3    Jaensch, L.4    Jahn, D.5    Schobert, M.6
  • 2
    • 43949108572 scopus 로고    scopus 로고
    • Corynebacterium glutamicum tailored for high-yield L-valine production
    • DOI 10.1007/s00253-008-1444-z
    • B Blombach ME Schreiner T Bartek M Oldiges BJ Eikmanns 2008 Corynebacterium glutamicum tailored for high-yield l-valine production Appl Microbiol Biotechnol 79 471 479 10.1007/s00253-008-1444-z 18379776 10.1007/s00253-008-1444-z 1:CAS:528:DC%2BD1cXlvF2kurs%3D (Pubitemid 351704103)
    • (2008) Applied Microbiology and Biotechnology , vol.79 , Issue.3 , pp. 471-479
    • Blombach, B.1    Schreiner, M.E.2    Bartek, T.3    Oldiges, M.4    Eikmanns, B.J.5
  • 3
    • 58149397920 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase, a novel target for improvement of l-lysine production by Corynebacterium glutamicum
    • 10.1128/aem.01844-08 19047397 10.1128/AEM.01844-08 1:CAS:528: DC%2BD1MXktlejsb8%3D
    • B Blombach S Hans B Bathe BJ Eikmanns 2009 Acetohydroxyacid synthase, a novel target for improvement of l-lysine production by Corynebacterium glutamicum Appl Environ Microbiol 75 419 427 10.1128/aem.01844-08 19047397 10.1128/AEM.01844-08 1:CAS:528:DC%2BD1MXktlejsb8%3D
    • (2009) Appl Environ Microbiol , vol.75 , pp. 419-427
    • Blombach, B.1    Hans, S.2    Bathe, B.3    Eikmanns, B.J.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • MM Bradford 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 942051 10.1016/0003-2697(76)90527-3 1:CAS:528: DyaE28XksVehtrY%3D
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 1542510099 scopus 로고    scopus 로고
    • Theoretical Foundation of the Balanced Minimum Evolution Method of Phylogenetic Inference and Its Relationship to Weighted Least-Squares Tree Fitting
    • DOI 10.1093/molbev/msh049
    • R Desper O Gascuel 2004 Theoretical foundation of the balanced minimum evolution method of phylogenetic inference and its relationship to weighted least-squares tree fitting Mol Biol Evol 21 3 587 598 10.1093/molbev.msh049 14694080 10.1093/molbev/msh049 1:CAS:528:DC%2BD2cXis1entb8%3D (Pubitemid 38339674)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.3 , pp. 587-598
    • Desper, R.1    Gascuel, O.2
  • 6
    • 12244275686 scopus 로고    scopus 로고
    • Feedback-resistant acetohydroxy acid synthase increases valine production in Corynebacterium glutamicum
    • DOI 10.1128/AEM.71.1.207-213.2005
    • V Elisakova M Patek J Holatko J Nesvera D Leyval JL Goergen S Delaunay 2005 Feedback-resistant acetohydroxy acid synthase increases valine production in Corynebacterium glutamicum Appl Environ Microbiol 71 207 213 10.1128/AEM.71.1.207-213.2005 15640189 10.1128/AEM.71.1.207-213.2005 1:CAS:528:DC%2BD2MXotlaqtg%3D%3D (Pubitemid 40116269)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.1 , pp. 207-213
    • Elisakova, V.1    Patek, M.2    Holatko, J.3    Nesvera, J.4    Leyval, D.5    Goergen, J.-L.6    Delaunay, S.7
  • 7
    • 41949141258 scopus 로고    scopus 로고
    • Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: Mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes
    • DOI 10.1128/JB.01831-07
    • ML Fernandez-Murga V Rubio 2008 Basis of arginine sensitivity of microbial N-acetyl-l-glutamate kinases: mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes J Bacteriol 190 3018 3025 10.1128/jb.01831-07 18263723 10.1128/JB.01831-07 1:CAS:528:DC%2BD1cXkslygsLg%3D (Pubitemid 351508202)
    • (2008) Journal of Bacteriology , vol.190 , Issue.8 , pp. 3018-3025
    • Fernandez-Murga, M.L.1    Rubio, V.2
  • 8
    • 4444234384 scopus 로고    scopus 로고
    • Arginine biosynthesis in Thermotoga maritima: Characterization of the arginine-sensitive N-acetyl-L-glutamate kinase
    • DOI 10.1128/JB.186.18.6142-6149.2004
    • ML Fernandez-Murga F Gil-Ortiz JL Llacer V Rubio 2004 Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-l-glutamate kinase J Bacteriol 186 6142 6149 10.1128/jb.186.18.6142- 6149.2004 15342584 10.1128/JB.186.18.6142-6149.2004 1:CAS:528: DC%2BD2cXns1eisbg%3D (Pubitemid 39187003)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6142-6149
    • Fernandez-Murga, M.L.1    Gil-Ortiz, F.2    Llacer, J.L.3    Rubio, V.4
  • 9
    • 24044432264 scopus 로고    scopus 로고
    • Lysine and glutamate production by Corynebacterium glutamicum on glucose, fructose and sucrose: Roles of malic enzyme and fructose-1,6-bisphosphatase
    • DOI 10.1016/j.ymben.2005.05.001, PII S1096717605000455
    • T Georgi D Rittmann VF Wendisch 2005 Lysine and glutamate production by Corynebacterium glutamicum on glucose, fructose and sucrose: roles of malic enzyme and fructose-1,6-bisphosphatase Metab Eng 7 291 301 10.1016/j.ymben.2005. 05.001 15979917 10.1016/j.ymben.2005.05.001 1:CAS:528:DC%2BD2MXpslymu7k%3D (Pubitemid 41225446)
    • (2005) Metabolic Engineering , vol.7 , Issue.4 , pp. 291-301
    • Georgi, T.1    Rittmann, D.2    Wendisch, V.F.3
  • 10
    • 0028818963 scopus 로고
    • Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites
    • 18345592 10.1007/BF00175826 1:CAS:528:DyaK2MXpsVKgtbo%3D
    • NV Grishin 1995 Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites J Mol Evol 41 5 675 679 18345592 10.1007/BF00175826 1:CAS:528:DyaK2MXpsVKgtbo%3D
    • (1995) J Mol Evol , vol.41 , Issue.5 , pp. 675-679
    • Grishin, N.V.1
  • 11
    • 0035667423 scopus 로고    scopus 로고
    • Metabolic redirection of carbon flow toward isoleucine by expressing a catabolic threonine dehydratase in a threonine-overproducing Corynebacterium glutamicum
    • DOI 10.1007/s00253-001-0829-z
    • S Guillouet A Rodal GH An P Lessard A Sinskey N Gorret 2001 Metabolic redirection of carbon flow toward isoleucine by expressing a catabolic threonine dehydratase in a threonine-overproducing Corynebacterium glutamicum Appl Microbiol Biotechnol 57 667 673 10.1007/s00253-001-0829-z 11778876 10.1007/s00253-001-0829-z 1:CAS:528:DC%2BD38Xhs1I%3D (Pubitemid 34028261)
    • (2001) Applied Microbiology and Biotechnology , vol.57 , Issue.5-6 , pp. 667-673
    • Guillouet, S.1    Rodal, A.2    An, G.-H.3    Gorret, N.4    Lessard, P.5    Sinskey, A.6
  • 12
    • 0015494346 scopus 로고
    • N-acetylglutamate synthetase of Pseudomonas aeruginosa. An assay in vitro and feedback inhibition by arginine
    • 10.1111/j.1432-1033.1972.tb02531.x 4630504 10.1111/j.1432-1033.1972. tb02531.x 1:CAS:528:DyaE3sXmvVKksg%3D%3D
    • D Haas V Kurer T Leisinger 1972 N-acetylglutamate synthetase of Pseudomonas aeruginosa. An assay in vitro and feedback inhibition by arginine Eur J Biochem 31 290 295 10.1111/j.1432-1033.1972.tb02531.x 4630504 10.1111/j.1432-1033.1972.tb02531.x 1:CAS:528:DyaE3sXmvVKksg%3D%3D
    • (1972) Eur J Biochem , vol.31 , pp. 290-295
    • Haas, D.1    Kurer, V.2    Leisinger, T.3
  • 14
    • 0037337416 scopus 로고    scopus 로고
    • The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis
    • DOI 10.1046/j.1432-1033.2003.03477.x
    • K Pauwels A Abadjieva P Hilven A Stankiewicz M Crabeel 2003 The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis Eur J Biochem 270 1014 1024 10.1046/j.1432-1033.2003. 03477.x 12603335 10.1046/j.1432-1033.2003.03477.x 1:CAS:528:DC%2BD3sXitlCmtbo%3D (Pubitemid 36315345)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.5 , pp. 1014-1024
    • Pauwels, K.1    Abadjieva, A.2    Hilven, P.3    Stankiewicz, A.4    Crabeel, M.5
  • 15
    • 0031860124 scopus 로고    scopus 로고
    • Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains
    • BS Rajagopal J DePonte 3rd M Tuchman MH Malamy 1998 Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains Appl Environ Microbiol 64 1805 1811 9572954 1:CAS:528:DyaK1cXislWls7Y%3D (Pubitemid 28234787)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.5 , pp. 1805-1811
    • Rajagopal, B.S.1    DePonte III, J.2    Tuchman, M.3    Malamy, M.H.4
  • 16
    • 31344471928 scopus 로고    scopus 로고
    • Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa
    • DOI 10.1016/j.jmb.2005.11.079, PII S0022283605015159
    • S Ramón-Maiques ML Fernández-Murga F Gil-Ortiz A Vagin I Fita V Rubio 2006 Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa J Mol Biol 356 695 713 10.1016/j.jmb.2005.11.079 16376937 10.1016/j.jmb.2005.11.079 (Pubitemid 43139330)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.3 , pp. 695-713
    • Ramon-Maiques, S.1    Fernandez-Murga, M.L.2    Gil-Ortiz, F.3    Vagin, A.4    Fita, I.5    Rubio, V.6
  • 17
    • 0030049883 scopus 로고    scopus 로고
    • Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: Enzyme evolution in the early steps of the arginine pathway
    • V Sakanyan P Petrosyan M Lecocq A Boyen C Legrain M Demarez JN Hallet N Glansdorff 1996 Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway Microbiol 142 Pt 1 99 108 10.1099/13500872-142-1-99 1:CAS:528:DyaK28XlsFOmtA%3D%3D (Pubitemid 26032051)
    • (1996) Microbiology , vol.142 , Issue.1 , pp. 99-108
    • Sakanyan, V.1    Petrosyan, P.2    Lecocq, M.3    Boyen, A.4    Legrain, C.5    Demarez, M.6    Hallet, J.-N.7    Glansdorff, N.8
  • 19
    • 26844567216 scopus 로고    scopus 로고
    • Genes, enzymes and regulation of arginine biosynthesis in plants
    • DOI 10.1016/j.plaphy.2005.06.007, PII S0981942805001671
    • R Slocum 2005 Genes, enzymes and regulation of arginine biosynthesis in plants Plant Phys Biochem 43 729 745 10.1016/j.plaphy.2005.06.007 10.1016/j.plaphy.2005.06.007 1:CAS:528:DC%2BD2MXhtFWhtr3K (Pubitemid 41454847)
    • (2005) Plant Physiology and Biochemistry , vol.43 , Issue.8 , pp. 729-745
    • Slocum, R.D.1
  • 20
    • 69249233521 scopus 로고    scopus 로고
    • Site-directed mutagenesis and computational study of the Y366 active site in Bacillus subtilis protoporphyrinogen oxidase
    • 10.1007/s00726-009-0256-5 19266155 10.1007/s00726-009-0256-5 1:CAS:528:DC%2BD1MXhtVaru73P
    • L Sun X Wen Y Tan H Li X Yang Y Zhao B Wang Q Cao C Niu Z Xi 2009 Site-directed mutagenesis and computational study of the Y366 active site in Bacillus subtilis protoporphyrinogen oxidase Amino Acids 37 523 530 10.1007/s00726-009-0256-5 19266155 10.1007/s00726-009-0256-5 1:CAS:528:DC%2BD1MXhtVaru73P
    • (2009) Amino Acids , vol.37 , pp. 523-530
    • Sun, L.1    Wen, X.2    Tan, Y.3    Li, H.4    Yang, X.5    Zhao, Y.6    Wang, B.7    Cao, Q.8    Niu, C.9    Xi, Z.10
  • 21
    • 4744362271 scopus 로고    scopus 로고
    • Production of arginine by fermentation
    • T Utagawa 2004 Production of arginine by fermentation J Natr 134 2854 2867
    • (2004) J Natr , vol.134 , pp. 2854-2867
    • Utagawa, T.1
  • 22
    • 33746927050 scopus 로고    scopus 로고
    • Genetic regulation of Corynebacterium glutamicum metabolism
    • VF Wendisch 2006 Genetic regulation of Corynebacterium glutamicum metabolism J Microbiol Biotechnol 16 999 1009 1:CAS:528:DC%2BD28XptlShtrc%3D (Pubitemid 44193277)
    • (2006) Journal of Microbiology and Biotechnology , vol.16 , Issue.7 , pp. 999-1009
    • Wendisch, V.F.1
  • 24
    • 56949102227 scopus 로고    scopus 로고
    • A two-stage oxygen supply strategy for enhanced l-arginine production by Corynebacterium crenatum based on metabolic fluxes analysis
    • 10.1016/j.bej.2008.08.007 10.1016/j.bej.2008.08.007 1:CAS:528: DC%2BD1cXhsVers7%2FF
    • H Xu W Dou H Xu X Zhang Z Rao Z Shi Z Xu 2009 A two-stage oxygen supply strategy for enhanced l-arginine production by Corynebacterium crenatum based on metabolic fluxes analysis Biochem Eng J 43 41 51 10.1016/j.bej.2008.08.007 10.1016/j.bej.2008.08.007 1:CAS:528:DC%2BD1cXhsVers7%2FF
    • (2009) Biochem Eng J , vol.43 , pp. 41-51
    • Xu, H.1    Dou, W.2    Xu, H.3    Zhang, X.4    Rao, Z.5    Shi, Z.6    Xu, Z.7
  • 25
    • 79952699344 scopus 로고    scopus 로고
    • Enhanced production of l-arginine by expression of Vitreoscilla hemoglobin using a novel expression system in Corynebacterium crenatum
    • 10.1007/s12010-010-9076-z 20835781 10.1007/s12010-010-9076-z 1:CAS:528:DC%2BC3MXisFylurs%3D
    • MJ Xu ZM Rao H Xu CY Lan WF Dou XM Zhang HY Xu JA Jin ZH Xu 2011 Enhanced production of l-arginine by expression of Vitreoscilla hemoglobin using a novel expression system in Corynebacterium crenatum Appl Biochem Biotechnol 163 707 719 10.1007/s12010-010-9076-z 20835781 10.1007/s12010-010-9076-z 1:CAS:528:DC%2BC3MXisFylurs%3D
    • (2011) Appl Biochem Biotechnol , vol.163 , pp. 707-719
    • Xu, M.J.1    Rao, Z.M.2    Xu, H.3    Lan, C.Y.4    Dou, W.F.5    Zhang, X.M.6    Xu, H.Y.7    Jin, J.A.8    Xu, Z.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.