메뉴 건너뛰기




Volumn 3, Issue 6, 1998, Pages 535-548

Functional analysis of the Escherichia coli genome for members of the α/β hydrolase family

Author keywords

Fold prediction; Function prediction; Functional genomics; Hydrolase family

Indexed keywords

HYDROLASE;

EID: 0032411227     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00069-8     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 0343569210 scopus 로고
    • Structure of human rhinovirus proteinase reveals a typsin-like polypeptide fold, RNA-binding site, and means for cleaving percusin polyprotein
    • Matthews, D.A., et al., & Worland, S. (1994). Structure of human rhinovirus proteinase reveals a typsin-like polypeptide fold, RNA-binding site, and means for cleaving percusin polyprotein. Cell 77, 1-20.
    • (1994) Cell , vol.77 , pp. 1-20
    • Matthews, D.A.1    Worland, S.2
  • 2
    • 0028567137 scopus 로고
    • Molecular evolution and domain structure of plasminogen-related growth factors (HGF/S and HGF1/MSP)
    • Donate, L.E., Gherardi, E., Srinivasan, N., Sowdhamini, R., Aparicio, S. & Blundell, T.L. (1994). Molecular evolution and domain structure of plasminogen-related growth factors (HGF/S and HGF1/MSP). Protein Sci. 3, 2378-2394.
    • (1994) Protein Sci. , vol.3 , pp. 2378-2394
    • Donate, L.E.1    Gherardi, E.2    Srinivasan, N.3    Sowdhamini, R.4    Aparicio, S.5    Blundell, T.L.6
  • 3
    • 0027050011 scopus 로고
    • Sequence-structure matching in globular proteins: Application to supersecondary and tertiary structure determination
    • Godzik, A. & Skolnick, J. (1992). Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination. Proc. Natl Acad. Sci. USA 89, 12098-12102.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 12098-12102
    • Godzik, A.1    Skolnick, J.2
  • 4
    • 0030067191 scopus 로고    scopus 로고
    • Assigning amino acid sequences to 3-dimensional protein folds
    • Fischer, D., Rice, D., Bowie, J.U. & Eisenberg, D. (1996). Assigning amino acid sequences to 3-dimensional protein folds. FASEB J. 10, 126-136.
    • (1996) FASEB J. , vol.10 , pp. 126-136
    • Fischer, D.1    Rice, D.2    Bowie, J.U.3    Eisenberg, D.4
  • 7
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S.F., et al., & Lipman, D.J. (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Lipman, D.J.2
  • 8
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R. & Lipman, D.J. (1988). Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 9
    • 0010612316 scopus 로고
    • Biocomputing Research Unit, University of Edinburgh, Edinburgh
    • Sturrock, S.S. & Colins, J.F. (1993). MPsrch version 1.3. Biocomputing Research Unit, University of Edinburgh, Edinburgh.
    • (1993) MPsrch Version 1.3
    • Sturrock, S.S.1    Colins, J.F.2
  • 10
  • 11
    • 0026410103 scopus 로고
    • Automated assembly of protein blocks for database searching
    • Henikoff, S. & Henikoff, J.G. (1991). Automated assembly of protein blocks for database searching. Nucleic Acids Res. 19, 6565-6572.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6565-6572
    • Henikoff, S.1    Henikoff, J.G.2
  • 12
    • 0028246722 scopus 로고
    • PRINTS - A protein motif fingerprint database
    • Attwood, T.K. & Beck, M.E. (1994). PRINTS - a protein motif fingerprint database. Protein Eng. 7, 841-848.
    • (1994) Protein Eng. , vol.7 , pp. 841-848
    • Attwood, T.K.1    Beck, M.E.2
  • 14
    • 0032483312 scopus 로고    scopus 로고
    • Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases
    • Fetrow, J.S. & Skolnick, J. (1998). Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases. J. Mol. Biol. 281, 949-968.
    • (1998) J. Mol. Biol. , vol.281 , pp. 949-968
    • Fetrow, J.S.1    Skolnick, J.2
  • 15
    • 0030874881 scopus 로고    scopus 로고
    • Upases and alpha/beta hydrolase fold
    • Schrag, J.D. & Cygler, M. (1997). Upases and alpha/beta hydrolase fold. Methods Enzymol. 284, 85-107.
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 16
    • 0026540411 scopus 로고
    • The α/β hydrolase fold
    • Ollis, D.L, et al., & Goldman, A. (1992). The α/β hydrolase fold. Protein Eng. 5, 197-211.
    • (1992) Protein Eng. , vol.5 , pp. 197-211
    • Ollis, D.L.1    Goldman, A.2
  • 17
    • 0031866670 scopus 로고    scopus 로고
    • aCHEdb: The database system for ESTHER, α/β fold family of proteins and the cholinesterase gene server
    • Cousin, X., Hotelier, T., Giles, K., Toutant, J.P. & Chatonnet, A. (1998). aCHEdb: the database system for ESTHER, α/β fold family of proteins and the cholinesterase gene server. Nucleic Acids Res. 26, 226-228.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 226-228
    • Cousin, X.1    Hotelier, T.2    Giles, K.3    Toutant, J.P.4    Chatonnet, A.5
  • 18
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L., et al., & Silman, I. (1991). Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Silman, I.2
  • 19
    • 0030589190 scopus 로고    scopus 로고
    • A pancreatic lipase with a phospholipase A1 activity: Crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig
    • Withers-Martinez, C., Carriere, F., Verger, R., Bourgeois, D. & Cambillau, C. (1996). A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure 4, 1363-1374.
    • (1996) Structure , vol.4 , pp. 1363-1374
    • Withers-Martinez, C.1    Carriere, F.2    Verger, R.3    Bourgeois, D.4    Cambillau, C.5
  • 20
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm, L. & Sander, C. (1997). Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res. 25, 231-234.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 21
    • 0030586027 scopus 로고    scopus 로고
    • Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • Wagner, U.G., Hasslacher, M., Griengl, H., Schwab, H. & Kratky, C. (1996). Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4, 811-822.
    • (1996) Structure , vol.4 , pp. 811-822
    • Wagner, U.G.1    Hasslacher, M.2    Griengl, H.3    Schwab, H.4    Kratky, C.5
  • 22
    • 0025734772 scopus 로고
    • Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken, S.M., Rozeboom, HJ., Kalk, K.H. & Dijkstra, B.W. (1991). Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. EMBO J. 10, 1297-1302.
    • (1991) EMBO J. , vol.10 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 23
    • 0031746105 scopus 로고    scopus 로고
    • Fold prediction by a hierarchy of sequence, threading, and modeling methods
    • Jaroszewski, L., Rychlewski, L., Zhang, B. & Godzik, A. (1998). Fold prediction by a hierarchy of sequence, threading, and modeling methods. Protein Sci. 7, 1431-1440.
    • (1998) Protein Sci. , vol.7 , pp. 1431-1440
    • Jaroszewski, L.1    Rychlewski, L.2    Zhang, B.3    Godzik, A.4
  • 24
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F.R., et al., & Shao, Y. (1997). The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1474.
    • (1997) Science , vol.277 , pp. 1453-1474
    • Blattner, F.R.1    Shao, Y.2
  • 25
    • 0028483211 scopus 로고
    • The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold
    • Hecht, H.J., Sobek, H., Haag, T., Reifer, O. & van Pee, K.-H. (1994). The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold. Nat. Struct. Biol. 1, 532-537.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 532-537
    • Hecht, H.J.1    Sobek, H.2    Haag, T.3    Reifer, O.4    Van Pee, K.-H.5
  • 26
    • 0030800827 scopus 로고    scopus 로고
    • Identification of important motifs in protein sequences: Program MULTIM and its applications to lipase-related sequences
    • Petersen, S.B., Drablos, F., Petersen, M.T. & Petersen, E.I. (1997). Identification of important motifs in protein sequences: program MULTIM and its applications to lipase-related sequences. Methods Enzymol. 284, 61-85.
    • (1997) Methods Enzymol. , vol.284 , pp. 61-85
    • Petersen, S.B.1    Drablos, F.2    Petersen, M.T.3    Petersen, E.I.4
  • 27
    • 0029973830 scopus 로고    scopus 로고
    • Derivation of 3-D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteinases and upases
    • Wallace, A.C., Laskowski, R.A. & Thornton, J.M. (1996). Derivation of 3-D coordinate templates for searching structural databases: application to Ser-His-Asp catalytic triads in the serine proteinases and upases. Protein Sci. 5, 1001-1013.
    • (1996) Protein Sci. , vol.5 , pp. 1001-1013
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 28
    • 0030724039 scopus 로고    scopus 로고
    • TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites
    • Wallace, A.C., Borkakoti, N. & Thornton, J.M. (1997). TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites. Protein Sci. 6, 2308-2323.
    • (1997) Protein Sci. , vol.6 , pp. 2308-2323
    • Wallace, A.C.1    Borkakoti, N.2    Thornton, J.M.3
  • 29
    • 0029046744 scopus 로고
    • An assessment of amino acid exchange matrices in aligning protein sequences: The twilight zone revisited
    • Vogt, G., Etzold, T. & Argos, P. (1995). An assessment of amino acid exchange matrices in aligning protein sequences: the twilight zone revisited. J. Mol. Biol. 249, 816-831.
    • (1995) J. Mol. Biol. , vol.249 , pp. 816-831
    • Vogt, G.1    Etzold, T.2    Argos, P.3
  • 30
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J.J. & Craik, C.S. (1995). Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 31
    • 0030470263 scopus 로고    scopus 로고
    • Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants
    • Longhi, S., et al., & Cambillau, C. (1996). Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins 26, 442-458.
    • (1996) Proteins , vol.26 , pp. 442-458
    • Longhi, S.1    Cambillau, C.2
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT, a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT, a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0030610593 scopus 로고    scopus 로고
    • Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae
    • Shilton, B.H., Thomas, D.Y. & Cygler, M. (1997). Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae. Biochemistry 36, 9002-9012.
    • (1997) Biochemistry , vol.36 , pp. 9002-9012
    • Shilton, B.H.1    Thomas, D.Y.2    Cygler, M.3
  • 34
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: Stereochemical analysis
    • Longhi, S., Czjzek, M., Lamzin, V., Nicolas, A. & Cambillau, C. (1997). Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: stereochemical analysis. J. Mol. Biol. 268, 779-799.
    • (1997) J. Mol. Biol. , vol.268 , pp. 779-799
    • Longhi, S.1    Czjzek, M.2    Lamzin, V.3    Nicolas, A.4    Cambillau, C.5
  • 35
    • 0030596528 scopus 로고    scopus 로고
    • Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution
    • Lang, D., et al., & Schomburg, D. (1996). Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution. J. Mol. Biol. 259, 704-717.
    • (1996) J. Mol. Biol. , vol.259 , pp. 704-717
    • Lang, D.1    Schomburg, D.2
  • 36
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • Pathak, D. & Ollis, D.L. (1990). Refined structure of dienelactone hydrolase at 1.8 Å. J. Mol. Biol. 214, 497-525.
    • (1990) J. Mol. Biol. , vol.214 , pp. 497-525
    • Pathak, D.1    Ollis, D.L.2
  • 37
    • 0024278449 scopus 로고
    • Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Rozeboom, H.J., Kingma, J., Janssen, D.B. & Dijkstra, B.W. (1988). Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Mol. Biol. 200, 611-612.
    • (1988) J. Mol. Biol. , vol.200 , pp. 611-612
    • Rozeboom, H.J.1    Kingma, J.2    Janssen, D.B.3    Dijkstra, B.W.4
  • 38
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg, J., Hansen, MX, Patkar, S. & Jones, T.A. (1994). The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2, 293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.X.2    Patkar, S.3    Jones, T.A.4
  • 39
    • 0028141817 scopus 로고
    • Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi
    • Lawson, D.M., et al., & Derewenda, Z.S. (1994). Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry 33, 9382-9388.
    • (1994) Biochemistry , vol.33 , pp. 9382-9388
    • Lawson, D.M.1    Derewenda, Z.S.2
  • 41
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 A resolution
    • Derewenda, Z.S., Derewenda, U. & Dodson, G.G. (1992). The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 A resolution. J. Mol. Biol. 227, 818-839.
    • (1992) J. Mol. Biol. , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 42
    • 0029645906 scopus 로고
    • Three-dimensional structure of the human 'protective protein': Structure of the precursor form suggests a complex activation mechanism
    • Rudenko, G., Bonten, E., d'Azzo, A. & Hol, W.G. (1995). Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism. Structure 3, 1249-1259.
    • (1995) Structure , vol.3 , pp. 1249-1259
    • Rudenko, G.1    Bonten, E.2    D'Azzo, A.3    Hol, W.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.