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Volumn 192, Issue 13, 2010, Pages 3287-3293

Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; BACTERIAL PROTEIN; COENZYME A; FRUCTOSE 6 PHOSPHATE; GLUCOSAMINE 1 PHOSPHATE; GLUCOSAMINE DERIVATIVE; GLUCOSE 1 PHOSPHATE THYMIDYLYLTRANSFERASE; N ACETYL DEXTRO GALACTOSAMINE 1 PHOSPHATE; NUCLEOTIDYLTRANSFERASE; PROTEIN ST0452; TRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URIDINE TRIPHOSPHATE;

EID: 77954379177     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01683-09     Document Type: Article
Times cited : (13)

References (31)
  • 3
    • 0034724727 scopus 로고    scopus 로고
    • Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association
    • Boehmelt, G., I. Fialka, G. Brothers, M. D. McGinley, S. D. Patterson, R. Mo, C. C. Hui, S. Chung, L. A. Huber, T. W. Mak, and N. N. Iscove. 2000. Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275:12821-12832.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12821-12832
    • Boehmelt, G.1    Fialka, I.2    Brothers, G.3    McGinley, M.D.4    Patterson, S.D.5    Mo, R.6    Hui, C.C.7    Chung, S.8    Huber, L.A.9    Mak, T.W.10    Iscove, N.N.11
  • 4
    • 27644571659 scopus 로고    scopus 로고
    • Two-step enzymatic synthesis of UDP-N-acetylgalactosamine
    • Bourgeaux, V., F. Piller, and V. Piller. 2005. Two-step enzymatic synthesis of UDP-N-acetylgalactosamine. Bioorg. Med. Chem. Lett. 15:5459-5462.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5459-5462
    • Bourgeaux, V.1    Piller, F.2    Piller, V.3
  • 5
    • 0033517131 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: A paradigm for the related pyrophosphorylase superfamily
    • Brown, K., F. Pompeo, S. Dixon, D. Mengin-Lecreulx, C. Cambillau, and Y. Bourne. 1999. Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. EMBO J. 18:4096-4107.
    • (1999) EMBO J. , vol.18 , pp. 4096-4107
    • Brown, K.1    Pompeo, F.2    Dixon, S.3    Mengin-Lecreulx, D.4    Cambillau, C.5    Bourne, Y.6
  • 6
    • 0034705422 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6
    • Creuzenet, C., M. Belanger, W. W. Wakarchuk, and J. S. Lam. 2000. Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6. J. Biol. Chem. 275:19060-19067.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19060-19067
    • Creuzenet, C.1    Belanger, M.2    Wakarchuk, W.W.3    Lam, J.S.4
  • 7
    • 0028209603 scopus 로고
    • Characterization of a human antigen with sera from infertile patients
    • Diekman, A. B., and E. Goldberg. 1994. Characterization of a human antigen with sera from infertile patients. Biol. Reprod. 50:1087-1093.
    • (1994) Biol. Reprod. , vol.50 , pp. 1087-1093
    • Diekman, A.B.1    Goldberg, E.2
  • 8
    • 0030051742 scopus 로고    scopus 로고
    • Acetyltransfer precedes uridylyltransfer in the formation of UDP-N- Acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli
    • DOI 10.1021/bi952275a
    • Gehring, A. M., W. J. Lees, D. J. Mindiola, C. T. Walsh, and E. D. Brown. 1996. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35:579-585. (Pubitemid 26032710)
    • (1996) Biochemistry , vol.35 , Issue.2 , pp. 579-585
    • Gehring, A.M.1    Lees, W.J.2    Mindiola, D.J.3    Walsh, C.T.4    Brown, E.D.5
  • 9
    • 33751250543 scopus 로고    scopus 로고
    • Biochemical characterization of UDP-GlcNAc/Glc 4-epimerase from Escherichia coli O86:B7
    • Guo, H. J., L. Li, and P. G. Wang. 2006. Biochemical characterization of UDP-GlcNAc/Glc 4-epimerase from Escherichia coli O86:B7. Biochemistry 45:13760-13768.
    • (2006) Biochemistry , vol.45 , pp. 13760-13768
    • Guo, H.J.1    Li, L.2    Wang, P.G.3
  • 10
    • 53449096114 scopus 로고    scopus 로고
    • GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability of Aspergillus fumigatus
    • Jiang, H., H. Ouyang, H. Zhou, and C. Jin. 2008. GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability of Aspergillus fumigatus. Microbiology 154:2730-2739.
    • (2008) Microbiology , vol.154 , pp. 2730-2739
    • Jiang, H.1    Ouyang, H.2    Zhou, H.3    Jin, C.4
  • 11
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuber ADP-glucose pyrophosphorylase
    • DOI 10.1038/sj.emboj.7600551
    • Jin, X., M. A. Ballicora, J. Preiss, and J. H. Geiger. 2005. Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO J. 24:694-704. (Pubitemid 40396100)
    • (2005) EMBO Journal , vol.24 , Issue.4 , pp. 694-704
    • Jin, X.1    Ballicora, M.A.2    Preies, J.3    Geiger, J.H.4
  • 12
    • 0029874435 scopus 로고    scopus 로고
    • A left-handed ß-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
    • Kisker, C., H. Schindelin, B. E. Alber, J. G. Ferry, and D. C. Rees. 1996. A left-handed ß-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 15:2323-2330.
    • (1996) EMBO J. , vol.15 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 14
    • 0030032719 scopus 로고    scopus 로고
    • Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli
    • Mengin-Lecreulx, D., and J. van Heijenoort. 1996. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 271:32-39.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32-39
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2
  • 15
    • 0027938707 scopus 로고
    • Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: Characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
    • Mengin-Lecreulx, D., and J. van Heijenoort. 1994. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176:5788-5795.
    • (1994) J. Bacteriol. , vol.176 , pp. 5788-5795
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2
  • 16
    • 32544436403 scopus 로고    scopus 로고
    • Enzymes of UDP-GlcNAc biosynthesis in yeast
    • Milewski, S., L. Gabriel, and J. Olchowy. 2006. Enzymes of UDP-GlcNAc biosynthesis in yeast. Yeast 23:1-14.
    • (2006) Yeast , vol.23 , pp. 1-14
    • Milewski, S.1    Gabriel, L.2    Olchowy, J.3
  • 17
    • 49049114041 scopus 로고    scopus 로고
    • Enzymatic analysis of UDP-N-acetylglucosamine
    • Namboori, S. C., and D. E. Graham. 2008. Enzymatic analysis of UDP-N-acetylglucosamine. Anal. Biochem. 381:94-100.
    • (2008) Anal. Biochem. , vol.381 , pp. 94-100
    • Namboori, S.C.1    Graham, D.E.2
  • 18
    • 41949094643 scopus 로고    scopus 로고
    • Acetamide sugar biosynthesis in the euryarchaea
    • Namboori, S. C., and D. E. Graham. 2008. Acetamide sugar biosynthesis in the euryarchaea. J. Bacteriol. 190:2987-2996.
    • (2008) J. Bacteriol. , vol.190 , pp. 2987-2996
    • Namboori, S.C.1    Graham, D.E.2
  • 19
    • 0035916240 scopus 로고    scopus 로고
    • Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
    • Olsen, L. R., and S. L. Roderick. 2001. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40:1913-1921.
    • (2001) Biochemistry , vol.40 , pp. 1913-1921
    • Olsen, L.R.1    Roderick, S.L.2
  • 20
    • 0029808206 scopus 로고    scopus 로고
    • Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation
    • Pastuszak, I., R. Drake, and A. D. Elbein. 1996. Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J. Biol. Chem. 271:20776-20782.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20776-20782
    • Pastuszak, I.1    Drake, R.2    Elbein, A.D.3
  • 21
    • 0031659702 scopus 로고    scopus 로고
    • Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: Site-directed mutagenesis and characterization of the mutant enzymes
    • Pompeo, F., J. van Heijenoort, and D. Mengin-Lecreulx. 1998. Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes. J. Bacteriol. 180:4799-4803.
    • (1998) J. Bacteriol. , vol.180 , pp. 4799-4803
    • Pompeo, F.1    Van Heijenoort, J.2    Mengin-Lecreulx, D.3
  • 22
    • 0028844306 scopus 로고
    • A left-handed parallel ß helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R. H., and S. L. Roderick. 1995. A left-handed parallel ß helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270:997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 24
    • 17144423209 scopus 로고    scopus 로고
    • Mediators of galactose sensitivity in UDP-galactose 4′-epimerase- impaired mammalian cells
    • Schulz, J. M., K. L. Ross, K. Malmstrom, M. Krieger, and J. L. Fridovich-Keil. 2005. Mediators of galactose sensitivity in UDP-galactose 4′-epimerase-impaired mammalian cells. J. Biol. Chem. 280:13493-13502.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13493-13502
    • Schulz, J.M.1    Ross, K.L.2    Malmstrom, K.3    Krieger, M.4    Fridovich-Keil, J.L.5
  • 25
    • 23744492608 scopus 로고    scopus 로고
    • Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- And UDP-glucose pyrophosphorylase activities
    • Silva, E., A. R. Marques, A. M. Fialho, A. T. Granja, and I. Sá-Correia. 2005. Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- and UDP-glucose pyrophosphorylase activities. Appl. Environ. Microbiol. 71:4703-4712.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4703-4712
    • Silva, E.1    Marques, A.R.2    Fialho, A.M.3    Granja, A.T.4    Sá-Correia, I.5
  • 26
    • 0035853790 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1- phosphate uridyltransferase bound to acetyl-coenzyme a reveals a novel active site architecture
    • Sulzenbacher, G., L. Gal, C. Peneff, F. Fassy, and Y. Bourne. 2001. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J. Biol. Chem. 276:11844-11851.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11844-11851
    • Sulzenbacher, G.1    Gal, L.2    Peneff, C.3    Fassy, F.4    Bourne, Y.5
  • 27
    • 15844428445 scopus 로고    scopus 로고
    • Purification to homogeneity and properties of UDP-GlcNAc (GalNAc) pyrophosphorylase
    • Szumilo, T., Y. Zeng, I. Pastuszak, R. Drake, H. Szumilo, and A. D. Elbein. 1996. Purification to homogeneity and properties of UDP-GlcNAc (GalNAc) pyrophosphorylase. J. Biol. Chem. 271:13147-13154.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13147-13154
    • Szumilo, T.1    Zeng, Y.2    Pastuszak, I.3    Drake, R.4    Szumilo, H.5    Elbein, A.D.6
  • 28
    • 25444511171 scopus 로고    scopus 로고
    • The molecular architecture of human N-acetylgalactosamine kinase
    • Thoden, J. B., and H. M. Holden. 2005. The molecular architecture of human N-acetylgalactosamine kinase. J. Biol. Chem. 280:32784-32791.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32784-32791
    • Thoden, J.B.1    Holden, H.M.2
  • 29
    • 0033977749 scopus 로고    scopus 로고
    • Identification and modification of the uridine-binding site of the UDP-GalNAc (GlcNAc) pyrophosphorylase
    • Wang-Gillam, A., I. Pastuszak, M. Stewart, R. R. Drake, and A. D. Elbein. 2000. Identification and modification of the uridine-binding site of the UDP-GalNAc (GlcNAc) pyrophosphorylase. J. Biol. Chem. 275:1433-1438.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1433-1438
    • Wang-Gillam, A.1    Pastuszak, I.2    Stewart, M.3    Drake, R.R.4    Elbein, A.D.5
  • 30
    • 38449095658 scopus 로고    scopus 로고
    • Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability
    • Zhang, Z., J. Akutsu, M. Tsujimura, and Y. Kawarabayasi. 2007. Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability. J. Biochem. 141:553-562.
    • (2007) J. Biochem. , vol.141 , pp. 553-562
    • Zhang, Z.1    Akutsu, J.2    Tsujimura, M.3    Kawarabayasi, Y.4
  • 31
    • 15744370966 scopus 로고    scopus 로고
    • Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic Archaeon, Sulfolobus tokodaii strain 7
    • Zhang, Z., M. Tsujimura, J. Akutsu, M. Sasaki, H. Tajima, and Y. Kawarabayasi. 2005. Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic Archaeon, Sulfolobus tokodaii strain 7. J. Biol. Chem. 280: 9698-9705.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9698-9705
    • Zhang, Z.1    Tsujimura, M.2    Akutsu, J.3    Sasaki, M.4    Tajima, H.5    Kawarabayasi, Y.6


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