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Volumn 44, Issue 17, 2005, Pages 6383-6391

Structural and catalytic diversity within the amidohydrolase superfamily

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; COMPLEXATION; HYDROLYSIS; MOLECULES; SUBSTRATES; X RAY CRYSTALLOGRAPHY;

EID: 17844384785     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047326v     Document Type: Review
Times cited : (330)

References (28)
  • 1
    • 0031000649 scopus 로고    scopus 로고
    • An Evolutionary Treasure: Unification of a Broad Set of Amidohydrolases Related to Urease
    • Holm, L., and Sander, C. (1997) An Evolutionary Treasure: Unification of a Broad Set of Amidohydrolases Related to Urease, Proteins: Struct., Funct., Genet. 28, 72-82.
    • (1997) Proteins: Struct., Funct., Genet. , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 2
    • 0032515956 scopus 로고    scopus 로고
    • Biochemical Characterization and Crystallographic Structure of an Escherichia coli Protein from the Phosphotriesterase Gene Family
    • Buchbinder, J. L., Stephenson, R. C., Dresser, M. J., Pitera, J. W., Scanlan, T. S., and Fletterick, R. J. (1998) Biochemical Characterization and Crystallographic Structure of an Escherichia coli Protein from the Phosphotriesterase Gene Family, Biochemistry 37, 5096-5106.
    • (1998) Biochemistry , vol.37 , pp. 5096-5106
    • Buchbinder, J.L.1    Stephenson, R.C.2    Dresser, M.J.3    Pitera, J.W.4    Scanlan, T.S.5    Fletterick, R.J.6
  • 4
    • 0035814923 scopus 로고    scopus 로고
    • High-Resolution X-ray Structures of Different Metal-Substituted Forms of Phosphotriesterase from Pseudomonas diminuta
    • Benning, M. M., Shim, H., Raushel, F. M., and Holden, H. M. (2001) High-Resolution X-ray Structures of Different Metal-Substituted Forms of Phosphotriesterase from Pseudomonas diminuta, Biochemistry 40, 2712-2722.
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 5
    • 0034730534 scopus 로고    scopus 로고
    • The Binding of Substrate Analogs to Phosphotriesterase
    • Benning, M. M., Hong, S.-B, Raushel, F. M., and Holden, H. M. (2000) The Binding of Substrate Analogs to Phosphotriesterase, J. Biol. Chem. 275, 30556-30560.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30556-30560
    • Benning, M.M.1    Hong, S.-B.2    Raushel, F.M.3    Holden, H.M.4
  • 6
    • 0033081891 scopus 로고    scopus 로고
    • A New Proposal for Urease Mechanism Based on the Crystal Structures of the Native and Inhibited Enzyme from Bacillus pasteurii: Why Urea Hydrolysis Costs Two Nickels
    • Benini, S., Rypniewski, W. R., Wilson, K. S., Miletti, S., Ciurli, S., and Mangani, S. (1999) A New Proposal for Urease Mechanism Based on the Crystal Structures of the Native and Inhibited Enzyme from Bacillus pasteurii: Why Urea Hydrolysis Costs Two Nickels, Struct. Folding Des. 7, 205-216.
    • (1999) Struct. Folding Des. , vol.7 , pp. 205-216
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 7
    • 0029647957 scopus 로고
    • The Crystal Structure of Urease from Klebsiella aerogenes
    • Jabri, E., Carr, M. B., Hausinger, R. P., and Karplus, P. A. (1995) The Crystal Structure of Urease from Klebsiella aerogenes, Science 268, 998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 8
    • 0035912842 scopus 로고    scopus 로고
    • Molecular Structure of Dihydroorotase: A Paradigm for Catalysis Through the Use of a Binuclear Metal Center
    • Thoden, J. B., Phillips, G. N., Jr., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular Structure of Dihydroorotase: A Paradigm for Catalysis Through the Use of a Binuclear Metal Center, Biochemistry 40, 6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips Jr., G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 9
    • 0038671973 scopus 로고    scopus 로고
    • High-Resolution X-ray Structure of Isoaspartyl Dipeptidase from Escherichia coli
    • Thoden, J. B., Marti-Arbona, R., Raushel, F. M., and Holden, H. M. (2003) High-Resolution X-ray Structure of Isoaspartyl Dipeptidase from Escherichia coli, Biochemistry 42, 4874-4882.
    • (2003) Biochemistry , vol.42 , pp. 4874-4882
    • Thoden, J.B.1    Marti-Arbona, R.2    Raushel, F.M.3    Holden, H.M.4
  • 10
    • 0036299882 scopus 로고    scopus 로고
    • X-ray Structure of a Dihydropyrimidinase from Thermus Sp. at 1.3 Å Resolution
    • Abendroth, J., Niefind, K., and Schomburg, D. (2002) X-ray Structure of a Dihydropyrimidinase from Thermus Sp. at 1.3 Å Resolution, J. Mol. Biol. 320, 143-156.
    • (2002) J. Mol. Biol. , vol.320 , pp. 143-156
    • Abendroth, J.1    Niefind, K.2    Schomburg, D.3
  • 11
    • 0037199453 scopus 로고    scopus 로고
    • Crystal Structure of D-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity
    • Cheon, Y. H., Kim, H. S., Han, K. H., Abendroth, J., Niefind, K., Schomburg, D., Wang, J., and Kim, Y. (2002) Crystal Structure of D-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity, Biochemistry 41, 9410-9417.
    • (2002) Biochemistry , vol.41 , pp. 9410-9417
    • Cheon, Y.H.1    Kim, H.S.2    Han, K.H.3    Abendroth, J.4    Niefind, K.5    Schomburg, D.6    Wang, J.7    Kim, Y.8
  • 12
    • 0037046968 scopus 로고    scopus 로고
    • The Structure of L-Hydantionase from Arthrobacter aurescens Leads to an Understanding of Dihydropyrimidinase Substrate and Enantio Specificity
    • Abendroth, J., Niefind, K., May, O., Siemann, M., Syldatk, C., and Schomburg, D. (2002) The Structure of L-Hydantionase from Arthrobacter aurescens Leads to an Understanding of Dihydropyrimidinase Substrate and Enantio Specificity, Biochemistry 41, 8589-8597.
    • (2002) Biochemistry , vol.41 , pp. 8589-8597
    • Abendroth, J.1    Niefind, K.2    May, O.3    Siemann, M.4    Syldatk, C.5    Schomburg, D.6
  • 13
    • 0036382767 scopus 로고    scopus 로고
    • Crystal Structure of Human Renal Dipeptidase Involved in Beta-Lactam Hydrolysis
    • Nitanai, Y., Satow, Y., Adachi, H., and Tsujimoto, M. (2002) Crystal Structure of Human Renal Dipeptidase Involved in Beta-Lactam Hydrolysis, J. Mol. Biol. 321, 177-184.
    • (2002) J. Mol. Biol. , vol.321 , pp. 177-184
    • Nitanai, Y.1    Satow, Y.2    Adachi, H.3    Tsujimoto, M.4
  • 14
    • 1642576068 scopus 로고    scopus 로고
    • The Three-Dimensional Structure of the N-Acetylglucosamine-6-Phosphate Deacetylase, NagA, from Bacillus subtilis: A Member of the Urease Superfamily
    • Vincent, F., Yates, D., Garman, E., Davies, G. J., and Brannigan, J. A. (2004) The Three-Dimensional Structure of the N-Acetylglucosamine-6-Phosphate Deacetylase, NagA, from Bacillus subtilis: A Member of the Urease Superfamily, J. Biol. Chem. 279, 2809-2816.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2809-2816
    • Vincent, F.1    Yates, D.2    Garman, E.3    Davies, G.J.4    Brannigan, J.A.5
  • 15
    • 0038701614 scopus 로고    scopus 로고
    • Crystal Structure of D-Aminoacylase from Alcaligenes faecalis Da1. A Novel Subset of Amidohydrolases and Insights into the Enzyme Mechanism
    • Liaw, S.-H., Chen, S.-J., Ko, T.-P., Hsu, C.-S., Chen, C. J., Wang, A. H., and Tsai, Y.-C. (2003) Crystal Structure of D-Aminoacylase from Alcaligenes faecalis Da1. A Novel Subset of Amidohydrolases and Insights into the Enzyme Mechanism, J. Biol. Chem. 278, 4957-4962.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4957-4962
    • Liaw, S.-H.1    Chen, S.-J.2    Ko, T.-P.3    Hsu, C.-S.4    Chen, C.J.5    Wang, A.H.6    Tsai, Y.-C.7
  • 16
    • 0032499630 scopus 로고    scopus 로고
    • Complexes of Adenosine Deaminase with Two Potent Inhibitors: X-ray Structures in Four Independent Molecules at pH of Maximum Activity
    • Wang, Z., and Quiocho, F. A. (1998) Complexes of Adenosine Deaminase with Two Potent Inhibitors: X-ray Structures in Four Independent Molecules at pH of Maximum Activity, Biochemistry 37, 8314-8324.
    • (1998) Biochemistry , vol.37 , pp. 8314-8324
    • Wang, Z.1    Quiocho, F.A.2
  • 17
  • 18
    • 0034720769 scopus 로고    scopus 로고
    • Self-Assembly of the Binuclear Metal Center of Phosphotriesterase
    • Shim, H., and Raushel, F. M. (2000) Self-Assembly of the Binuclear Metal Center of Phosphotriesterase, Biochemistry 39, 7357-7364.
    • (2000) Biochemistry , vol.39 , pp. 7357-7364
    • Shim, H.1    Raushel, F.M.2
  • 19
    • 0025106239 scopus 로고
    • Sequence of the Klebsiella aerogenes Urease Genes and Evidence for Accessory Proteins Facilitating Nickel Incorporation
    • Mulrooney, S. B., and Hausinger, R. P. (1990) Sequence of the Klebsiella aerogenes Urease Genes and Evidence for Accessory Proteins Facilitating Nickel Incorporation, J. Bacteriol. 172, 5837-5849.
    • (1990) J. Bacteriol. , vol.172 , pp. 5837-5849
    • Mulrooney, S.B.1    Hausinger, R.P.2
  • 20
    • 0026434561 scopus 로고
    • Atomic Structure of Adenosine Deaminase Complexed with a Transition State Analog: Understanding Catalysis and Immunodeficiency Mutations
    • Wilson, D. K., Rudolph, F. B., and Quiocho, F. A. (1991) Atomic Structure of Adenosine Deaminase Complexed with a Transition State Analog: Understanding Catalysis and Immunodeficiency Mutations, Science 252, 1278-1284.
    • (1991) Science , vol.252 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 21
    • 0027488896 scopus 로고
    • Cytosine Deaminase: The Roles of Divalent Metal Ions in Catalysis
    • Porter, D. J., and Austin, E. A. (1993). Cytosine Deaminase: The Roles of Divalent Metal Ions in Catalysis, J. Biol. Chem. 268, 24005-24011.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24005-24011
    • Porter, D.J.1    Austin, E.A.2
  • 22
    • 1842690128 scopus 로고    scopus 로고
    • The Functional Role of the Binuclear Metal Center in D-Aminoacylase - One-Metal Activation and Second-Metal Attenuation
    • Lai W. L., Chou, L. Y., Ting, C. Y., Kirby, R., Tsai, Y. C., Wang, A. H. J., and Liaw, S. H. (2004), The Functional Role of the Binuclear Metal Center in D-Aminoacylase - One-Metal Activation and Second-Metal Attenuation,J. Biol. Chem. 279, 13962-13967.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13962-13967
    • Lai, W.L.1    Chou, L.Y.2    Ting, C.Y.3    Kirby, R.4    Tsai, Y.C.5    Wang, A.H.J.6    Liaw, S.H.7
  • 23
    • 0028609492 scopus 로고
    • The Three-Dimensional Structure of Phosphotriesterase: An Enzyme Capable of Detoxifying Organophosphorus Nerve Agents
    • Benning, M. M., Kuo, J. M., Raushel, F. M., and Holden, H. M. (1994) The Three-Dimensional Structure of Phosphotriesterase: An Enzyme Capable of Detoxifying Organophosphorus Nerve Agents, Biochemistry 33, 15001-15007.
    • (1994) Biochemistry , vol.33 , pp. 15001-15007
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 24
    • 2442496666 scopus 로고    scopus 로고
    • Mechanism for the Hydrolysis of Organophosphates by the Bacterial Phosphotriesterase
    • Aubert, S. D., Li, Y., and Raushel, F. M. (2004) Mechanism for the Hydrolysis of Organophosphates by the Bacterial Phosphotriesterase, Biochemistry 43, 5707-5715.
    • (2004) Biochemistry , vol.43 , pp. 5707-5715
    • Aubert, S.D.1    Li, Y.2    Raushel, F.M.3
  • 25
    • 11144301188 scopus 로고    scopus 로고
    • Mechanism for the Dihydroorotase Reaction
    • Porter, T. N., Li, Y., and Raushel, F. M. (2004) Mechanism for the Dihydroorotase Reaction, Biochemistry 43, 16285-16292.
    • (2004) Biochemistry , vol.43 , pp. 16285-16292
    • Porter, T.N.1    Li, Y.2    Raushel, F.M.3
  • 26
    • 0035174756 scopus 로고    scopus 로고
    • Structure-based Rationalization of Urease Inhibition by Phosphate: Novel Insights into the Enzyme Mechanism
    • Benini, S, Rypniewski, W. R., Wilson, K. S., and Ciurli, S. (2001) Structure-based Rationalization of Urease Inhibition by Phosphate: Novel Insights into the Enzyme Mechanism, J. Biol. Inorg. Chem. 6, 778-790.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 778-790
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Ciurli, S.4
  • 28
    • 0035980264 scopus 로고    scopus 로고
    • Rapid Evolution of Bacterial Catabolic Enzymes: A Case Study with Atrazine Chlorohydrolase
    • Seffernick, J. L., and Wackett, L. P. (2001) Rapid Evolution of Bacterial Catabolic Enzymes: A Case Study with Atrazine Chlorohydrolase, Biochemistry 40, 12747-12753.
    • (2001) Biochemistry , vol.40 , pp. 12747-12753
    • Seffernick, J.L.1    Wackett, L.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.