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Volumn 12, Issue 5, 2008, Pages 532-538

Transient oxidation as a mechanistic strategy in enzymatic catalysis

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOGLUCOSIDASE DERIVATIVE; ADENOSINE DIPHOSPHATE LEVO GLYCERO DEXTRO MANNO HEPTOSE 6 EPIMERASE; EPIMERASE; GLUCOSIDASE; GUANOSINE DIPHOSPHATE MANNOSE 3,5 EPIMERASE; NICOTINAMIDE DERIVATIVE; RACEMASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 53849136554     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.06.016     Document Type: Review
Times cited : (8)

References (41)
  • 1
    • 0001555950 scopus 로고
    • Complex pyridine nucleotide-dependent transformations
    • Dolphin D., Poulson R., and Avramovic O. (Eds), Wiley
    • Frey P.A. Complex pyridine nucleotide-dependent transformations. In: Dolphin D., Poulson R., and Avramovic O. (Eds). Pyridine Nucleotide Coenzymes vol 2B (1987), Wiley 462-511
    • (1987) Pyridine Nucleotide Coenzymes , vol.2 B , pp. 462-511
    • Frey, P.A.1
  • 2
    • 0036919327 scopus 로고    scopus 로고
    • Flavoenzymes that catalyse reactions with no net redox change
    • Bornemann S. Flavoenzymes that catalyse reactions with no net redox change. Nat Prod Rep 19 (2002) 761-772
    • (2002) Nat Prod Rep , vol.19 , pp. 761-772
    • Bornemann, S.1
  • 3
    • 4644237751 scopus 로고    scopus 로고
    • Enzymatic reactions involving novel mechanisms of carbanion stabilization
    • Begley T.P., and Ealick S.E. Enzymatic reactions involving novel mechanisms of carbanion stabilization. Curr Opin Chem Biol 8 (2004) 508-515
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 508-515
    • Begley, T.P.1    Ealick, S.E.2
  • 4
    • 0035984275 scopus 로고    scopus 로고
    • Mechanistic aspects of enzymatic carbohydrate epimerization
    • Samuel J., and Tanner M.E. Mechanistic aspects of enzymatic carbohydrate epimerization. Nat Prod Rep 19 (2002) 261-277
    • (2002) Nat Prod Rep , vol.19 , pp. 261-277
    • Samuel, J.1    Tanner, M.E.2
  • 6
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway
    • Frey P.A. The Leloir pathway. FASEB J 10 (1996) 461-470
    • (1996) FASEB J , vol.10 , pp. 461-470
    • Frey, P.A.1
  • 7
    • 0017598377 scopus 로고
    • Fluorescence and nucleotide binding properties of Escherichia coli uridine diphoshate galactose 4-epimerase: support for a model for nonstereospecific action
    • Wong S.S., and Frey P.A. Fluorescence and nucleotide binding properties of Escherichia coli uridine diphoshate galactose 4-epimerase: support for a model for nonstereospecific action. Biochemistry 16 (1977) 298-305
    • (1977) Biochemistry , vol.16 , pp. 298-305
    • Wong, S.S.1    Frey, P.A.2
  • 8
    • 0032544212 scopus 로고    scopus 로고
    • Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from E. coli
    • Thoden J.B., and Holden H.M. Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from E. coli. Biochemistry 37 (1998) 11469-11477
    • (1998) Biochemistry , vol.37 , pp. 11469-11477
    • Thoden, J.B.1    Holden, H.M.2
  • 9
    • 0030832007 scopus 로고    scopus 로고
    • Mechanistic roles of tyrosine 149 and serine 124 in UDP galactose 4-epimerase from Escherichia coli
    • Liu Y., Thoden J.B., Kim J., Berger E., Gulick A.M., Ruzicka F.J., Holden H.M., and Frey P.A. Mechanistic roles of tyrosine 149 and serine 124 in UDP galactose 4-epimerase from Escherichia coli. Biochemistry 36 (1997) 10675-10684
    • (1997) Biochemistry , vol.36 , pp. 10675-10684
    • Liu, Y.1    Thoden, J.B.2    Kim, J.3    Berger, E.4    Gulick, A.M.5    Ruzicka, F.J.6    Holden, H.M.7    Frey, P.A.8
  • 10
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
    • Thoden J.B., Wohlers T.M., Fridovich-Keil J.L., and Holden H.M. Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry 39 (2000) 5691-5701
    • (2000) Biochemistry , vol.39 , pp. 5691-5701
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 11
    • 0036066728 scopus 로고    scopus 로고
    • Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
    • Valvano M.A., Messner P., and Kosma P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979-1989
    • (2002) Microbiology , vol.148 , pp. 1979-1989
    • Valvano, M.A.1    Messner, P.2    Kosma, P.3
  • 12
    • 0028071785 scopus 로고
    • Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosugar epimerase, ADP-l-glycero-d-manno-heptose 6-epimerase
    • Ding L., Seto B.L., Ahmed S.A., and Coleman Jr. W.G. Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosugar epimerase, ADP-l-glycero-d-manno-heptose 6-epimerase. J Biol Chem 269 (1994) 24384-24390
    • (1994) J Biol Chem , vol.269 , pp. 24384-24390
    • Ding, L.1    Seto, B.L.2    Ahmed, S.A.3    Coleman Jr., W.G.4
  • 13
    • 0034658405 scopus 로고    scopus 로고
    • The crystal structure of ADP-l-glycero-d-manno-heptose 6-epimerase: catalysis with a twist
    • Deacon A.M., Ni Y.S., Coleman W.G., and Ealick S.E. The crystal structure of ADP-l-glycero-d-manno-heptose 6-epimerase: catalysis with a twist. Structure 8 (2000) 453-462
    • (2000) Structure , vol.8 , pp. 453-462
    • Deacon, A.M.1    Ni, Y.S.2    Coleman, W.G.3    Ealick, S.E.4
  • 15
    • 3242745131 scopus 로고    scopus 로고
    • The mechanism of the reaction catalyzed by ADP-β-l-glycero-d-manno-heptose 6-epimerase
    • This paper provides the first evidence in support of a direct oxidation/reduction mechanism for ADP-heptose 6-epimerase.
    • Read J.A., Ahmed R.A., Morrison J.P., Coleman Jr. W.G., and Tanner M.E. The mechanism of the reaction catalyzed by ADP-β-l-glycero-d-manno-heptose 6-epimerase. J Am Chem Soc 126 (2004) 8878-8879. This paper provides the first evidence in support of a direct oxidation/reduction mechanism for ADP-heptose 6-epimerase.
    • (2004) J Am Chem Soc , vol.126 , pp. 8878-8879
    • Read, J.A.1    Ahmed, R.A.2    Morrison, J.P.3    Coleman Jr., W.G.4    Tanner, M.E.5
  • 16
    • 20544440615 scopus 로고    scopus 로고
    • Efficient chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose and a mechanistic study of ADP-l-glycero-d-manno-heptose 6-epimerase
    • Read J.A., Ahmed R.A., and Tanner M.E. Efficient chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose and a mechanistic study of ADP-l-glycero-d-manno-heptose 6-epimerase. Org Lett 7 (2005) 2457-2460
    • (2005) Org Lett , vol.7 , pp. 2457-2460
    • Read, J.A.1    Ahmed, R.A.2    Tanner, M.E.3
  • 17
    • 17144370967 scopus 로고    scopus 로고
    • Dismutase activity of ADP-l-glycero-d-manno-heptose 6-epimerase: evidence for a direct oxidation/reduction mechanism
    • This paper describes the use of an intermediate analog to provide the first direct evidence for a C-6″ oxidation process.
    • Morrison J.P., Read J.A., Coleman Jr. W.G., and Tanner M.E. Dismutase activity of ADP-l-glycero-d-manno-heptose 6-epimerase: evidence for a direct oxidation/reduction mechanism. Biochemistry 44 (2005) 5907-5915. This paper describes the use of an intermediate analog to provide the first direct evidence for a C-6″ oxidation process.
    • (2005) Biochemistry , vol.44 , pp. 5907-5915
    • Morrison, J.P.1    Read, J.A.2    Coleman Jr., W.G.3    Tanner, M.E.4
  • 18
    • 34249102543 scopus 로고    scopus 로고
    • Intermediate release by ADP-l-glycero-d-manno-heptose 6-epimerase
    • This paper demonstrates that hydride transfer is intramolecular and describes the trapping and identification of the 6″-keto intermediate.
    • Mayer A., and Tanner M.E. Intermediate release by ADP-l-glycero-d-manno-heptose 6-epimerase. Biochemistry 46 (2007) 6149-6155. This paper demonstrates that hydride transfer is intramolecular and describes the trapping and identification of the 6″-keto intermediate.
    • (2007) Biochemistry , vol.46 , pp. 6149-6155
    • Mayer, A.1    Tanner, M.E.2
  • 19
    • 33947653721 scopus 로고    scopus 로고
    • A two-base mechanism for Escherichia coli ADP-l-glycero-d-manno-heptose 6-epimerase
    • This paper establishes that two acid/base residues are required for nonstereospecific hydride transfer. It clearly distinguishes the mechanistic strategy employed by ADP-heptose 6-epimerase from that employed by UDP-galactose 4-epimerase.
    • Morrison J.P., and Tanner M.E. A two-base mechanism for Escherichia coli ADP-l-glycero-d-manno-heptose 6-epimerase. Biochemistry 46 (2007) 3916-3924. This paper establishes that two acid/base residues are required for nonstereospecific hydride transfer. It clearly distinguishes the mechanistic strategy employed by ADP-heptose 6-epimerase from that employed by UDP-galactose 4-epimerase.
    • (2007) Biochemistry , vol.46 , pp. 3916-3924
    • Morrison, J.P.1    Tanner, M.E.2
  • 20
    • 0034326439 scopus 로고    scopus 로고
    • New insights into the mechanism of CDP-tyvelose 2-epimerase: an enzyme catalyzing epimerization at an unactivated stereocenter
    • Hallis T.M., Zhao Z., and Liu H.-W. New insights into the mechanism of CDP-tyvelose 2-epimerase: an enzyme catalyzing epimerization at an unactivated stereocenter. J Am Chem Soc 122 (2000) 10493-10503
    • (2000) J Am Chem Soc , vol.122 , pp. 10493-10503
    • Hallis, T.M.1    Zhao, Z.2    Liu, H.-W.3
  • 21
    • 0038419490 scopus 로고    scopus 로고
    • High resolution X-ray structure of tyvelose epimerase from Salmonella typhi
    • Koropatkin N.M., Liu H.-W., and Holden H.M. High resolution X-ray structure of tyvelose epimerase from Salmonella typhi. J Biol Chem 278 (2003) 20847-20881
    • (2003) J Biol Chem , vol.278 , pp. 20847-20881
    • Koropatkin, N.M.1    Liu, H.-W.2    Holden, H.M.3
  • 22
    • 0036005636 scopus 로고    scopus 로고
    • Understanding nature's strategies for enzyme-catalyzed racemization and epimerization
    • Tanner M.E. Understanding nature's strategies for enzyme-catalyzed racemization and epimerization. Acc Chem Res 35 (2002) 237-246
    • (2002) Acc Chem Res , vol.35 , pp. 237-246
    • Tanner, M.E.1
  • 23
    • 29844441434 scopus 로고    scopus 로고
    • Structure and function of GDP-mannose-3′,5′-epimerase: an enzyme which performs three chemical reactions at the same active site
    • This paper provides structural snapshots along the epimerase reaction pathway and sets a framework for understanding how a complex transformation can be catalyzed within a single active site.
    • Major L.L., Wolucka B.A., and Naismith J.H. Structure and function of GDP-mannose-3′,5′-epimerase: an enzyme which performs three chemical reactions at the same active site. J Am Chem Soc 127 (2005) 18309-18320. This paper provides structural snapshots along the epimerase reaction pathway and sets a framework for understanding how a complex transformation can be catalyzed within a single active site.
    • (2005) J Am Chem Soc , vol.127 , pp. 18309-18320
    • Major, L.L.1    Wolucka, B.A.2    Naismith, J.H.3
  • 24
    • 0018801234 scopus 로고
    • Observations on the mechanism of the reversible epimerization of GDP-d-mannose to GDP-l-galactose by an enzyme from Chlorella pyrenoidosa
    • Barber G.A. Observations on the mechanism of the reversible epimerization of GDP-d-mannose to GDP-l-galactose by an enzyme from Chlorella pyrenoidosa. J Biol Chem 254 (1979) 7600-7603
    • (1979) J Biol Chem , vol.254 , pp. 7600-7603
    • Barber, G.A.1
  • 25
    • 0017124134 scopus 로고
    • Mechanism for enzymatic thioether formation
    • Palmer J.L., and Abeles R.H. Mechanism for enzymatic thioether formation. J Biol Chem 251 (1976) 5817-5819
    • (1976) J Biol Chem , vol.251 , pp. 5817-5819
    • Palmer, J.L.1    Abeles, R.H.2
  • 26
    • 33645213849 scopus 로고    scopus 로고
    • Breakdown of oligosaccharides by the process of elimination
    • Yip V.L.Y., and Withers S.G. Breakdown of oligosaccharides by the process of elimination. Curr Opin Chem Biol 10 (2006) 147-155
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 147-155
    • Yip, V.L.Y.1    Withers, S.G.2
  • 27
    • 0032538629 scopus 로고    scopus 로고
    • The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase
    • Thompson J., Pikis A., Ruvinov S.B., Henrissat B., Yamamoto H., and Sekiguchi J. The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase. J Biol Chem 273 (1998) 27347-27356
    • (1998) J Biol Chem , vol.273 , pp. 27347-27356
    • Thompson, J.1    Pikis, A.2    Ruvinov, S.B.3    Henrissat, B.4    Yamamoto, H.5    Sekiguchi, J.6
  • 28
    • 3142761743 scopus 로고    scopus 로고
    • An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 β-glycosidase from Thermatoga maritima
    • This paper provides the first evidence in support of a transient oxidation mechanism for the family 4 glycosidases.
    • Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., Anderson W.F., and Withers S.G. An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 β-glycosidase from Thermatoga maritima. J Am Chem Soc 126 (2004) 8354-8355. This paper provides the first evidence in support of a transient oxidation mechanism for the family 4 glycosidases.
    • (2004) J Am Chem Soc , vol.126 , pp. 8354-8355
    • Yip, V.L.Y.1    Varrot, A.2    Davies, G.J.3    Rajan, S.S.4    Yang, X.5    Thompson, J.6    Anderson, W.F.7    Withers, S.G.8
  • 29
    • 30744478437 scopus 로고    scopus 로고
    • Mechanistic analysis of the unusual redox-elimination sequence employed by Thermatoga maritima BglT: a 6-phospho-β-glucosidase from glycoside hydrolase family 4
    • This paper demonstrates that the elimination reactions in the family 4 glycosidases proceed in a stepwise fashion via enolate intermediates.
    • Yip V.L.Y., and Withers S.G. Mechanistic analysis of the unusual redox-elimination sequence employed by Thermatoga maritima BglT: a 6-phospho-β-glucosidase from glycoside hydrolase family 4. Biochemistry 45 (2006) 571-580. This paper demonstrates that the elimination reactions in the family 4 glycosidases proceed in a stepwise fashion via enolate intermediates.
    • (2006) Biochemistry , vol.45 , pp. 571-580
    • Yip, V.L.Y.1    Withers, S.G.2
  • 30
    • 12544256751 scopus 로고    scopus 로고
    • + and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-β-d-glucosides
    • This paper provides structural insight into an understanding of the mechanism catalyzed by the family 4 glycosidases.
    • + and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-β-d-glucosides. J Mol Biol 346 (2005) 423-435. This paper provides structural insight into an understanding of the mechanism catalyzed by the family 4 glycosidases.
    • (2005) J Mol Biol , vol.346 , pp. 423-435
    • Varrot, A.1    Yip, V.Y.L.2    Li, Y.3    Rajan, S.S.4    Yang, X.5    Anderson, W.F.6    Thompson, J.7    Withers, S.G.8    Davies, G.J.9
  • 31
    • 34548287921 scopus 로고    scopus 로고
    • Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-α-glucosidase from glycoside hydrolase family 4
    • Yip V.Y.L., Thompson J., and Withers S.G. Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-α-glucosidase from glycoside hydrolase family 4. Biochemistry 46 (2007) 9840-9852
    • (2007) Biochemistry , vol.46 , pp. 9840-9852
    • Yip, V.Y.L.1    Thompson, J.2    Withers, S.G.3
  • 35
    • 33749036332 scopus 로고    scopus 로고
    • Family 4 glycosidases carry out efficient hydrolysis of thioglycosides by an α,β-elimination mechanism
    • This paper highlights the unique mechanism employed by the family 4 glycosidases by demonstrating that they possess thioglycosidase activity.
    • Yip V.L.Y., and Withers S.G. Family 4 glycosidases carry out efficient hydrolysis of thioglycosides by an α,β-elimination mechanism. Angew Chem Int Ed 45 (2006) 6179-6182. This paper highlights the unique mechanism employed by the family 4 glycosidases by demonstrating that they possess thioglycosidase activity.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 6179-6182
    • Yip, V.L.Y.1    Withers, S.G.2
  • 36
    • 0036771816 scopus 로고    scopus 로고
    • Mechanisms of enzymatic C-O bond cleavages in deoxyhexose biosynthesis
    • He X., and Liu H.-W. Mechanisms of enzymatic C-O bond cleavages in deoxyhexose biosynthesis. Curr Opin Chem Biol 6 (2002) 590-597
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 590-597
    • He, X.1    Liu, H.-W.2
  • 37
    • 0035834048 scopus 로고    scopus 로고
    • Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis
    • Bar-Peled M., Griffith C.L., and Doering T.L. Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis. Proc Natl Acad Sci U S A 98 (2001) 12003-12008
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12003-12008
    • Bar-Peled, M.1    Griffith, C.L.2    Doering, T.L.3
  • 38
    • 0024517021 scopus 로고
    • Dehydroquinate synthase: a sheep in wolf's clothing?
    • Widlanksi T., Bender S.L., and Knowles J.R. Dehydroquinate synthase: a sheep in wolf's clothing?. J Am Chem Soc 111 (1989) 2299-2300
    • (1989) J Am Chem Soc , vol.111 , pp. 2299-2300
    • Widlanksi, T.1    Bender, S.L.2    Knowles, J.R.3
  • 39
    • 0001650027 scopus 로고
    • Does dehydroquinate synthase synthesize dehydroquinate?
    • Bartlett P.A., and Satake K. Does dehydroquinate synthase synthesize dehydroquinate?. J Am Chem Soc 110 (1988) 1628-1630
    • (1988) J Am Chem Soc , vol.110 , pp. 1628-1630
    • Bartlett, P.A.1    Satake, K.2
  • 40
    • 1842790985 scopus 로고    scopus 로고
    • +-2-deoxy-d-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism
    • +-2-deoxy-d-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism. J Biol Chem 279 (2004) 13889-13895
    • (2004) J Biol Chem , vol.279 , pp. 13889-13895
    • Jin, X.1    Foley, K.M.2    Geiger, J.H.3
  • 41
    • 0029921058 scopus 로고    scopus 로고
    • Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism
    • Thoden J.B., Frey P.A., and Holden H.M. Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism. Biochemistry 35 (1996) 5137-5144
    • (1996) Biochemistry , vol.35 , pp. 5137-5144
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3


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