메뉴 건너뛰기




Volumn 30, Issue 1, 2002, Pages 45-50

The most proficient enzyme as the central theme in an integrated, research-based biochemistry laboratory course

Author keywords

(Bradford) protein assay; Affinity chromatography; Bacterial complementation; Enzyme assays; Escherichia coli; Gene libraries; Orotidine 5 monophosphate decarboxylase; Pyrimidine metabolism; Saccharomyces cerevisiae; Spectrophotometry

Indexed keywords

ENZYME; OROTIDINE 5' PHOSPHATE DECARBOXYLASE;

EID: 22944439508     PISSN: 14708175     EISSN: None     Source Type: Journal    
DOI: 10.1002/bmb.2002.494030010008     Document Type: Article
Times cited : (5)

References (41)
  • 3
    • 2042457193 scopus 로고    scopus 로고
    • The buzz about a remarkable enzyme
    • A. M. Rouhi (2000) The buzz about a remarkable enzyme, Chem. Eng. News 78, 42-46.
    • (2000) Chem. Eng. News , vol.78 , pp. 42-46
    • Rouhi, A.M.1
  • 4
    • 10044293452 scopus 로고    scopus 로고
    • Editor's choice: Highlights from the recent literature
    • G. Chin (2000) Editor's choice: highlights from the recent literature, Science 288, 401-403.
    • (2000) Science , vol.288 , pp. 401-403
    • Chin, G.1
  • 5
    • 0034519315 scopus 로고    scopus 로고
    • Catalysis and regulation; clarity through structures
    • J. Stubbe, L. N. Johnson (2000) Catalysis and regulation; clarity through structures, Curr. Opin. Struct. Biol. 10, 709-710.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 709-710
    • Stubbe, J.1    Johnson, L.N.2
  • 6
    • 0035793649 scopus 로고    scopus 로고
    • Circe effect versus enzyme preorganization: What can be learned from the structure of the most proficient enzyme?
    • A. Warshel, J. Florian, M. Strabel, J. Villa (2001) Circe effect versus enzyme preorganization: what can be learned from the structure of the most proficient enzyme? ChemBioChem 2, 109-111.
    • (2001) ChemBioChem , vol.2 , pp. 109-111
    • Warshel, A.1    Florian, J.2    Strabel, M.3    Villa, J.4
  • 7
    • 0035793646 scopus 로고    scopus 로고
    • Crystal structures of orotidine monophosphate decarboxylase: Does the structure reveal the mechanism of nature's most proficient enzyme?
    • K. N. Houk, J. K. Lee, D. J. Tantillo, S. Bahmanyar, B. N. Hietbrink (2001) Crystal structures of orotidine monophosphate decarboxylase: does the structure reveal the mechanism of nature's most proficient enzyme? ChemBioChem 2, 113-118.
    • (2001) ChemBioChem , vol.2 , pp. 113-118
    • Houk, K.N.1    Lee, J.K.2    Tantillo, D.J.3    Bahmanyar, S.4    Hietbrink, B.N.5
  • 8
    • 0026517477 scopus 로고
    • The orotidine-5′-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family
    • H. H. Kimsey, D. Kaiser (1992) The orotidine-5′-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family, J. Biol. Chem. 267, 819-824.
    • (1992) J. Biol. Chem. , vol.267 , pp. 819-824
    • Kimsey, H.H.1    Kaiser, D.2
  • 9
    • 0028918401 scopus 로고
    • A proficient enzyme
    • A. Radzicka, R. Wolfenden (1995) A proficient enzyme, Science 267, 90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 10
    • 0035574727 scopus 로고    scopus 로고
    • A re-examination of the substrate utilization of 2-thioorotidine- 5′-monophosphate by yeast OMP decarboxylase
    • J. A. Smiley, K. M. Hay, B. S. Levison (2001) A re-examination of the substrate utilization of 2-thioorotidine-5′-monophosphate by yeast OMP decarboxylase, Bioorg. Chem. 29, 96-106.
    • (2001) Bioorg. Chem. , vol.29 , pp. 96-106
    • Smiley, J.A.1    Hay, K.M.2    Levison, B.S.3
  • 11
    • 0035805488 scopus 로고    scopus 로고
    • Dissecting a charged network at the active site of orotidine-5′- phosphate decarboxylase
    • B. G. Miller, M. J. Snider, R. Wolfenden, S. A. Short (2001) Dissecting a charged network at the active site of orotidine-5′-phosphate decarboxylase, J. Biol. Chem. 276, 15174-15176.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15174-15176
    • Miller, B.G.1    Snider, M.J.2    Wolfenden, R.3    Short, S.A.4
  • 12
    • 0034682613 scopus 로고    scopus 로고
    • Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5′-phosphate decarboxylase
    • B. G. Miller, M. J. Snider, S. A. Short, R. Wolfenden (2000) Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5′-phosphate decarboxylase, Biochemistry 39, 8113-8118.
    • (2000) Biochemistry , vol.39 , pp. 8113-8118
    • Miller, B.G.1    Snider, M.J.2    Short, S.A.3    Wolfenden, R.4
  • 13
    • 0034718457 scopus 로고    scopus 로고
    • Yeast orotidine-5′-phosphate decarboxylase: Steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation
    • D. J. Porter, S. A. Short (2000) Yeast orotidine-5′-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation, Biochemistry 39, 11788-11800.
    • (2000) Biochemistry , vol.39 , pp. 11788-11800
    • Porter, D.J.1    Short, S.A.2
  • 14
    • 0038998655 scopus 로고    scopus 로고
    • Determination of the mechanism of orotidine-5′-monophosphate decarboxylase by isotope effects
    • M. A. Rishavy, W. W. Cleland (2000) Determination of the mechanism of orotidine-5′-monophosphate decarboxylase by isotope effects, Biochemistry 39, 4569-4574.
    • (2000) Biochemistry , vol.39 , pp. 4569-4574
    • Rishavy, M.A.1    Cleland, W.W.2
  • 15
    • 0034058368 scopus 로고    scopus 로고
    • The crystal structure and mechanism of orotidine-5′-monophosphate decarboxylase
    • T. C. Appleby, C. Kinsland, T. P. Begley, S. E. Ealick (2000) The crystal structure and mechanism of orotidine-5′-monophosphate decarboxylase, Proc. Nat. Acad. Sci. U. S. A. 97, 2005-2010.
    • (2000) Proc. Nat. Acad. Sci. U. S. A. , vol.97 , pp. 2005-2010
    • Appleby, T.C.1    Kinsland, C.2    Begley, T.P.3    Ealick, S.E.4
  • 16
    • 0034104285 scopus 로고    scopus 로고
    • Anatomy of a proficient enzyme: The structure of orotidine-5′- monophosphate decarboxylase in the presence and absence of a potential transition state analog
    • B. G. Miller, A. M. Hassell, R. Wolfenden, M. V. Milburn, S. A. Short (2000) Anatomy of a proficient enzyme: the structure of orotidine-5′- monophosphate decarboxylase in the presence and absence of a potential transition state analog, Proc. Nat. Acad. Sci U. S. A. 97, 2011-2016.
    • (2000) Proc. Nat. Acad. Sci U. S. A. , vol.97 , pp. 2011-2016
    • Miller, B.G.1    Hassell, A.M.2    Wolfenden, R.3    Milburn, M.V.4    Short, S.A.5
  • 17
    • 0034102419 scopus 로고    scopus 로고
    • Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylase
    • N. Wu, Y. Mo, J. Gao, E. F. Pai (2000) Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase, Proc. Nat. Acad. Sci. U. S. A. 97, 2017-2022.
    • (2000) Proc. Nat. Acad. Sci. U. S. A. , vol.97 , pp. 2017-2022
    • Wu, N.1    Mo, Y.2    Gao, J.3    Pai, E.F.4
  • 18
    • 0034681950 scopus 로고    scopus 로고
    • Structural basis for the catalytic mechanism of a proficient enzyme: Orotidine-5′-monophosphate decarboxylase
    • P. Harris, J. C. Navarro-Poulsen, K. F. Jensen, S. Larsen (2000) Structural basis for the catalytic mechanism of a proficient enzyme: orotidine-5′-monophosphate decarboxylase, Biochemistry 39, 4217-4224.
    • (2000) Biochemistry , vol.39 , pp. 4217-4224
    • Harris, P.1    Navarro-Poulsen, J.C.2    Jensen, K.F.3    Larsen, S.4
  • 19
    • 0000264492 scopus 로고    scopus 로고
    • The mechanism of orotidine-5′-monophosphate decarboxylase: Catalysis by destabilization of the substrate
    • W. Y. Feng, T. J. Austin, F. Chew, S. Gronert, W. Wu (2000) The mechanism of orotidine-5′-monophosphate decarboxylase: catalysis by destabilization of the substrate, Biochemistry 39, 1778-1783.
    • (2000) Biochemistry , vol.39 , pp. 1778-1783
    • Feng, W.Y.1    Austin, T.J.2    Chew, F.3    Gronert, S.4    Wu, W.5
  • 20
    • 0034610398 scopus 로고    scopus 로고
    • Remarkable rate enhancement of orotidine-5′-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization
    • A. Warshel, M. Strajbl, J. Villa, J. Florian (2000) Remarkable rate enhancement of orotidine-5′-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization, Biochemistry 39, 14728-14738.
    • (2000) Biochemistry , vol.39 , pp. 14728-14738
    • Warshel, A.1    Strajbl, M.2    Villa, J.3    Florian, J.4
  • 22
    • 0032817361 scopus 로고    scopus 로고
    • Active site probes for yeast OMP decarboxylase: Inhibition constants of UMP and thio-substituted UMP analogues and greatly reduced activity toward CMP-6-carboxylate
    • J. A. Smiley, L. Saleh (1999) Active site probes for yeast OMP decarboxylase: inhibition constants of UMP and thio-substituted UMP analogues and greatly reduced activity toward CMP-6-carboxylate, Bioorg. Chem. 27, 297-306.
    • (1999) Bioorg. Chem. , vol.27 , pp. 297-306
    • Smiley, J.A.1    Saleh, L.2
  • 23
    • 0033588155 scopus 로고    scopus 로고
    • Activity of yeast orotidine-5′-phosphate decarboxylase in the absence of metals
    • B. G. Miller, J. A. Smiley, S. A. Short, R. Wolfenden (1999) Activity of yeast orotidine-5′-phosphate decarboxylase in the absence of metals, J. Biol. Chem. 274, 23841-23843.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23841-23843
    • Miller, B.G.1    Smiley, J.A.2    Short, S.A.3    Wolfenden, R.4
  • 25
    • 0030912339 scopus 로고    scopus 로고
    • A proficient enzyme revisited: The predicted mechanism for orotidine monophosphate decarboxylase
    • J. K. Lee, K. N. Houk (1997) A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase, Science 276, 942-945.
    • (1997) Science , vol.276 , pp. 942-945
    • Lee, J.K.1    Houk, K.N.2
  • 26
    • 0028938397 scopus 로고
    • Expression of an orotate decarboxylating catalytic antibody confers 5-fluoro-orotate sensitivity to a pyrimidine auxotrophic Escherichia coli: An example of intracellular prodrug activation
    • J. A. Smiley, S. J. Benkovic (1995) Expression of an orotate decarboxylating catalytic antibody confers 5-fluoro-orotate sensitivity to a pyrimidine auxotrophic Escherichia coli: an example of intracellular prodrug activation, J. Am. Chem. Soc. 117, 3877-3878.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3877-3878
    • Smiley, J.A.1    Benkovic, S.J.2
  • 27
    • 0028068780 scopus 로고
    • Selection of catalytic antibodies for a biosynthetic reaction from a combinatorial cDNA library by complementation of an auxotrophic Escherichia coli: Antibodies for orotate decarboxylation
    • J. A. Smiley, S. J. Benkovic (1994) Selection of catalytic antibodies for a biosynthetic reaction from a combinatorial cDNA library by complementation of an auxotrophic Escherichia coli: antibodies for orotate decarboxylation, Proc. Natl. Acad. Sci U. S. A. 91, 8319-8323.
    • (1994) Proc. Natl. Acad. Sci U. S. A. , vol.91 , pp. 8319-8323
    • Smiley, J.A.1    Benkovic, S.J.2
  • 28
    • 0026622110 scopus 로고
    • A unique catalytic and inhibitor-binding role for Lys93 of yeast orotidylate decarboxylase
    • J. A. Smiley, M. E. Jones (1992) A unique catalytic and inhibitor-binding role for Lys93 of yeast orotidylate decarboxylase, Biochemistry 31, 12162-12168.
    • (1992) Biochemistry , vol.31 , pp. 12162-12168
    • Smiley, J.A.1    Jones, M.E.2
  • 29
    • 0026677723 scopus 로고
    • Orotidylate decarboxylase: Insights into the catalytic mechanism from substrate-specificity studies
    • K. Shostak, M. E. Jones (1992) Orotidylate decarboxylase: insights into the catalytic mechanism from substrate-specificity studies, Biochemistry 31, 12155-12161.
    • (1992) Biochemistry , vol.31 , pp. 12155-12161
    • Shostak, K.1    Jones, M.E.2
  • 30
    • 0025775806 scopus 로고
    • Investigation of the enzymatic mechanism of yeast orotidine-5′- monophosphate decarboxylase using C-13 kinetic isotope effects
    • J. A. Smiley, P. Paneth, M. H. O'Leary, J. B. Bell, M. E. Jones (1991) Investigation of the enzymatic mechanism of yeast orotidine-5′- monophosphate decarboxylase using C-13 kinetic isotope effects, Biochemistry 30, 6216-6223.
    • (1991) Biochemistry , vol.30 , pp. 6216-6223
    • Smiley, J.A.1    Paneth, P.2    O'Leary, M.H.3    Bell, J.B.4    Jones, M.E.5
  • 31
    • 0025272740 scopus 로고
    • Orotidine-5′-monophosphate decarboxylase catalysis: Kinetic isotope effects and the state of hybridization of a bound transition-state analog
    • S. A. Acheson, J. B. Bell, M. E. Jones, R. Wolfenden (1990) Orotidine-5′-monophosphate decarboxylase catalysis: kinetic isotope effects and the state of hybridization of a bound transition-state analog, Biochemistry 29, 3198-3202.
    • (1990) Biochemistry , vol.29 , pp. 3198-3202
    • Acheson, S.A.1    Bell, J.B.2    Jones, M.E.3    Wolfenden, R.4
  • 32
    • 0019334745 scopus 로고
    • Inhibition of orotidine-5′-phosphate decarboxylase by 1-(5′-phospho-β-D-ribofuranosyl)barbituric acid, 6-azauridine 5′-phosphate, and uridine 5′- phosphate
    • H. L. Levine, R. S. Brody, F. H. Westheimer (1980) Inhibition of orotidine-5′-phosphate decarboxylase by 1-(5′-phospho-β-D- ribofuranosyl)barbituric acid, 6-azauridine 5′-phosphate, and uridine 5′- phosphate, Biochemistry 19, 4993-4999.
    • (1980) Biochemistry , vol.19 , pp. 4993-4999
    • Levine, H.L.1    Brody, R.S.2    Westheimer, F.H.3
  • 33
    • 0017302117 scopus 로고
    • Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine-5′-phosphate decarboxylase
    • P. Beak, B. Siegel (1976) Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine-5′-phosphate decarboxylase, J. Am. Chem. Soc. 98, 3601-3606.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3601-3606
    • Beak, P.1    Siegel, B.2
  • 34
    • 0025874328 scopus 로고
    • Purification and characterization of yeast orotidine 5′- monophosphate decarboxylase overexpressed from plasmid pGU2
    • J. B. Bell, M. E. Jones (1991) Purification and characterization of yeast orotidine 5′-monophosphate decarboxylase overexpressed from plasmid pGU2, J. Biol. Chem. 266, 12662-12667.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12662-12667
    • Bell, J.B.1    Jones, M.E.2
  • 35
    • 0018169995 scopus 로고
    • Conversion of uridine nucleotides to the 6-cyano derivatives: Synthesis of orotidylic acid
    • T. Ueda, M. Yamamoto, A. Yamane, M. Imazawa, H. Ioue (1978) Conversion of uridine nucleotides to the 6-cyano derivatives: synthesis of orotidylic acid, J. Carbohydr. 5, 261-271.
    • (1978) J. Carbohydr. , vol.5 , pp. 261-271
    • Ueda, T.1    Yamamoto, M.2    Yamane, A.3    Imazawa, M.4    Ioue, H.5
  • 36
    • 0022511769 scopus 로고
    • Sequence analysis of the pyr-4 (orotidine-5′-phosphate decarboxylase) gene of Neurospora crassa
    • S. F. Newbury, J. A. Glazebrook, A. Radford (1986) Sequence analysis of the pyr-4 (orotidine-5′-phosphate decarboxylase) gene of Neurospora crassa, Gene (Amst.) 43, 51-58.
    • (1986) Gene (Amst.) , vol.43 , pp. 51-58
    • Newbury, S.F.1    Glazebrook, J.A.2    Radford, A.3
  • 38
    • 0004270170 scopus 로고
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, K. Struhl, Eds., Greene Publishing Associates and John Wiley & Sons, Inc., New York
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, K. Struhl, Eds. (1994) Current Protocols in Molecular Biology, Greene Publishing Associates and John Wiley & Sons, Inc., New York.
    • (1994) Current Protocols in Molecular Biology
  • 39
    • 0018362441 scopus 로고
    • The purification of orotidine-5′-phosphate decarboxylase from yeast by affinity chromatography
    • R. S. Brody, F. H. Westheimer (1979) The purification of orotidine-5′-phosphate decarboxylase from yeast by affinity chromatography, J. Biol. Chem. 254, 4238-4244.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4238-4244
    • Brody, R.S.1    Westheimer, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.