메뉴 건너뛰기




Volumn 20, Issue 5, 2010, Pages 543-550

Biosynthetic enzymes of unusual microbial sugars

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; AMINOTRANSFERASE; BACTERIUM LIPOPOLYSACCHARIDE; CARBOHYDRATE; ERYTHROMYCIN; GLUCOSE 6 PHOSPHATASE; MONOSACCHARIDE;

EID: 78049428649     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.08.002     Document Type: Review
Times cited : (19)

References (29)
  • 1
    • 57549105096 scopus 로고    scopus 로고
    • Natural-product sugar biosynthesis and enzymatic glycodiversification
    • Thibodeaux C.J., Melancon C.E., Liu H.W. Natural-product sugar biosynthesis and enzymatic glycodiversification. Angew Chem Int Ed Engl 2008, 47:9814-9859.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 9814-9859
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.W.3
  • 2
    • 34247626294 scopus 로고    scopus 로고
    • Unusual sugar biosynthesis and natural product glycodiversification
    • Thibodeaux C.J., Melancon C.E., Liu H.W. Unusual sugar biosynthesis and natural product glycodiversification. Nature 2007, 446:1008-1016.
    • (2007) Nature , vol.446 , pp. 1008-1016
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.W.3
  • 3
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz C.R., Roderick S.L. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 1995, 270:997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.1    Roderick, S.L.2
  • 4
    • 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., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y. Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. EMBO J 1999, 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
  • 5
    • 0035916240 scopus 로고    scopus 로고
    • Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
    • Olsen L.R., Roderick S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 2001, 40:1913-1921.
    • (2001) Biochemistry , vol.40 , pp. 1913-1921
    • Olsen, L.R.1    Roderick, S.L.2
  • 6
    • 0035847005 scopus 로고    scopus 로고
    • Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2. 33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1. 96Å resolution
    • Kostrewa D., D'Arcy A., Takacs B., Kamber M. Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2. 33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1. 96Å resolution. J Mol Biol 2001, 305:279-289.
    • (2001) J Mol Biol , vol.305 , pp. 279-289
    • Kostrewa, D.1    D'Arcy, A.2    Takacs, B.3    Kamber, M.4
  • 7
    • 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., Gal L., Peneff C., Fassy F., Bourne Y. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J Biol Chem 2001, 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
  • 8
    • 39649117771 scopus 로고    scopus 로고
    • Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni
    • Rangarajan E.S., Ruane K.M., Sulea T., Watson D.C., Proteau A., Leclerc S., Cygler M., Matte A., Young N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 2008, 47:1827-1836.
    • (2008) Biochemistry , vol.47 , pp. 1827-1836
    • Rangarajan, E.S.1    Ruane, K.M.2    Sulea, T.3    Watson, D.C.4    Proteau, A.5    Leclerc, S.6    Cygler, M.7    Matte, A.8    Young, N.M.9
  • 9
    • 55549145055 scopus 로고    scopus 로고
    • Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni
    • Olivier N.B., Imperiali B. Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni. J Biol Chem 2008, 283:27937-27946.
    • (2008) J Biol Chem , vol.283 , pp. 27937-27946
    • Olivier, N.B.1    Imperiali, B.2
  • 10
    • 65249154793 scopus 로고    scopus 로고
    • Structural and functional studies of QdtC: an N-acetyltransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-d-glucose
    • Thoden J.B., Cook P.D., Schaffer C., Messner P., Holden H.M. Structural and functional studies of QdtC: an N-acetyltransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-d-glucose. Biochemistry 2009, 48:2699-2709.
    • (2009) Biochemistry , vol.48 , pp. 2699-2709
    • Thoden, J.B.1    Cook, P.D.2    Schaffer, C.3    Messner, P.4    Holden, H.M.5
  • 11
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski C.M., Wren B.W. Protein glycosylation in bacterial mucosal pathogens. Nat Rev Microbiol 2005, 3:225-237.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 12
    • 66349134115 scopus 로고    scopus 로고
    • Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni
    • Demendi M., Creuzenet C: Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni. Biochem Cell Biol 2009, 87:469-483.
    • (2009) Biochem Cell Biol , vol.87 , pp. 469-483
    • Demendi, M.1    Creuzenet, C.2
  • 13
    • 77953097504 scopus 로고    scopus 로고
    • Molecular structure of WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-d-mannuronic acid
    • Thoden J.B., Holden H.M. Molecular structure of WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-d-mannuronic acid. Biochemistry 2010.
    • (2010) Biochemistry
    • Thoden, J.B.1    Holden, H.M.2
  • 15
    • 33646827681 scopus 로고    scopus 로고
    • Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori
    • Schoenhofen I.C., Lunin V.V., Julien J.P., Li Y., Ajamian E., Matte A., Cygler M., Brisson J.R., Aubry A., Logan S.M., et al. Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori. J Biol Chem 2006, 281:8907-8916.
    • (2006) J Biol Chem , vol.281 , pp. 8907-8916
    • Schoenhofen, I.C.1    Lunin, V.V.2    Julien, J.P.3    Li, Y.4    Ajamian, E.5    Matte, A.6    Cygler, M.7    Brisson, J.R.8    Aubry, A.9    Logan, S.M.10
  • 16
    • 34247632529 scopus 로고    scopus 로고
    • Molecular architecture of DesV from Streptomyces venezuelae: a PLP-dependent transaminase involved in the biosynthesis of the unusual sugar desosamine
    • Burgie E.S., Thoden J.B., Holden H.M. Molecular architecture of DesV from Streptomyces venezuelae: a PLP-dependent transaminase involved in the biosynthesis of the unusual sugar desosamine. Protein Sci 2007, 16:887-896.
    • (2007) Protein Sci , vol.16 , pp. 887-896
    • Burgie, E.S.1    Thoden, J.B.2    Holden, H.M.3
  • 17
    • 34547726112 scopus 로고    scopus 로고
    • Molecular architecture of DesI: a key enzyme in the biosynthesis of desosamine
    • Burgie E.S., Holden H.M. Molecular architecture of DesI: a key enzyme in the biosynthesis of desosamine. Biochemistry 2007, 46:8999-9006.
    • (2007) Biochemistry , vol.46 , pp. 8999-9006
    • Burgie, E.S.1    Holden, H.M.2
  • 18
    • 40149092973 scopus 로고    scopus 로고
    • GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar
    • Cook P.D., Holden H.M. GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar. Biochemistry 2008, 47:2833-2840.
    • (2008) Biochemistry , vol.47 , pp. 2833-2840
    • Cook, P.D.1    Holden, H.M.2
  • 19
    • 53249103318 scopus 로고    scopus 로고
    • Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase
    • Cook P.D., Carney A.E., Holden H.M. Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase. Biochemistry 2008, 47:10685-10693.
    • (2008) Biochemistry , vol.47 , pp. 10685-10693
    • Cook, P.D.1    Carney, A.E.2    Holden, H.M.3
  • 20
    • 61749087768 scopus 로고    scopus 로고
    • Structural analysis of QdtB, an aminotransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-d-glucose
    • Thoden J.B., Schaffer C., Messner P., Holden H.M. Structural analysis of QdtB, an aminotransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-d-glucose. Biochemistry 2009, 48:1553-1561.
    • (2009) Biochemistry , vol.48 , pp. 1553-1561
    • Thoden, J.B.1    Schaffer, C.2    Messner, P.3    Holden, H.M.4
  • 21
    • 0032514668 scopus 로고    scopus 로고
    • A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity
    • Xue Y., Zhao L., Liu H.W., Sherman D.H. A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity. Proc Natl Acad Sci U S A 1998, 95:12111-12116.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12111-12116
    • Xue, Y.1    Zhao, L.2    Liu, H.W.3    Sherman, D.H.4
  • 22
    • 33748199595 scopus 로고    scopus 로고
    • The structure of GDP-4-keto-6-deoxy-d-mannose-3-dehydratase: a unique coenzyme B6-dependent enzyme
    • Cook P.D., Thoden J.B., Holden H.M. The structure of GDP-4-keto-6-deoxy-d-mannose-3-dehydratase: a unique coenzyme B6-dependent enzyme. Protein Sci 2006, 15:2093-2106.
    • (2006) Protein Sci , vol.15 , pp. 2093-2106
    • Cook, P.D.1    Thoden, J.B.2    Holden, H.M.3
  • 23
    • 37049019111 scopus 로고    scopus 로고
    • A structural study of GDP-4-keto-6-deoxy-d-mannose-3-dehydratase: caught in the act of geminal diamine formation
    • Cook P.D., Holden H.M. A structural study of GDP-4-keto-6-deoxy-d-mannose-3-dehydratase: caught in the act of geminal diamine formation. Biochemistry 2007, 46:14215-14224.
    • (2007) Biochemistry , vol.46 , pp. 14215-14224
    • Cook, P.D.1    Holden, H.M.2
  • 24
    • 42949104259 scopus 로고    scopus 로고
    • GDP-4-keto-6-deoxy-d-mannose 3-dehydratase, accommodating a sugar substrate in the active site
    • Cook P.D., Holden H.M. GDP-4-keto-6-deoxy-d-mannose 3-dehydratase, accommodating a sugar substrate in the active site. J Biol Chem 2008, 283:4295-4303.
    • (2008) J Biol Chem , vol.283 , pp. 4295-4303
    • Cook, P.D.1    Holden, H.M.2
  • 25
    • 0028818689 scopus 로고
    • Sequence and analysis of the O antigen gene (rfb) cluster of Escherichia coli O111
    • Bastin D.A., Reeves P.R. Sequence and analysis of the O antigen gene (rfb) cluster of Escherichia coli O111. Gene 1995, 164:17-23.
    • (1995) Gene , vol.164 , pp. 17-23
    • Bastin, D.A.1    Reeves, P.R.2
  • 26
    • 0037621444 scopus 로고    scopus 로고
    • The biosynthesis of GDP-l-colitose: C-3 deoxygenation is catalyzed by a unique coenzyme B6-dependent enzyme
    • Beyer N., Alam J., Hallis T.M., Guo Z., Liu H.W. The biosynthesis of GDP-l-colitose: C-3 deoxygenation is catalyzed by a unique coenzyme B6-dependent enzyme. J Am Chem Soc 2003, 125:5584-5585.
    • (2003) J Am Chem Soc , vol.125 , pp. 5584-5585
    • Beyer, N.1    Alam, J.2    Hallis, T.M.3    Guo, Z.4    Liu, H.W.5
  • 27
    • 11144320397 scopus 로고    scopus 로고
    • Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-d-mannose-3-dehydrase (ColD) and GDP-l-colitose synthase (ColC)
    • Alam J., Beyer N., Liu H.W. Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-d-mannose-3-dehydrase (ColD) and GDP-l-colitose synthase (ColC). Biochemistry 2004, 43:16450-16460.
    • (2004) Biochemistry , vol.43 , pp. 16450-16460
    • Alam, J.1    Beyer, N.2    Liu, H.W.3
  • 28
    • 67049119446 scopus 로고    scopus 로고
    • Two site-directed mutations are required for the conversion of a sugar dehydratase into an aminotransferase
    • Cook P.D., Kubiak R.L., Toomey D.P., Holden H.M. Two site-directed mutations are required for the conversion of a sugar dehydratase into an aminotransferase. Biochemistry 2009, 48:5246-5253.
    • (2009) Biochemistry , vol.48 , pp. 5246-5253
    • Cook, P.D.1    Kubiak, R.L.2    Toomey, D.P.3    Holden, H.M.4
  • 29
    • 45749107783 scopus 로고    scopus 로고
    • Structure and mutagenic conversion of E1 dehydrase: at the crossroads of dehydration, amino transfer, and epimerization
    • Smith P., Szu P.H., Bui C., Liu H.W., Tsai S.C. Structure and mutagenic conversion of E1 dehydrase: at the crossroads of dehydration, amino transfer, and epimerization. Biochemistry 2008, 47:6329-6341.
    • (2008) Biochemistry , vol.47 , pp. 6329-6341
    • Smith, P.1    Szu, P.H.2    Bui, C.3    Liu, H.W.4    Tsai, S.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.