메뉴 건너뛰기




Volumn 292, Issue 1, 1999, Pages 11-17

The Zn-peptidase superfamily: Functional convergence after evolutionary divergence

Author keywords

Aminopeptidase; Aspartoacylase; Carboxypeptidase; Protease; Succinylglutamate desuccinylase

Indexed keywords

AMIDASE; ASPARTOACYLASE; BACTERIAL ENZYME; CARBOXYPEPTIDASE; HYDROLASE; SUCCINYLGLUTAMATE DESUCCINYLASE; UNCLASSIFIED DRUG;

EID: 0033543723     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3059     Document Type: Article
Times cited : (90)

References (32)
  • 1
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases
    • Altschul S. F., Koonin E. V. Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases. Trends Biochem. Sci. 23:1998;444-447.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 3
    • 0032509884 scopus 로고    scopus 로고
    • Eukaryotic transcription regulators derive from ancient enzymatic domains
    • Aravind L., Koonin E. V. Eukaryotic transcription regulators derive from ancient enzymatic domains. Curr. Biol. 8:1998;R111-R113.
    • (1998) Curr. Biol. , vol.8
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind L., Koonin E. V. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287:1999;1023-1040.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 5
    • 0026553106 scopus 로고
    • Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques
    • Artymiuk P. J., Grindley H. M., Park J. E., Rice D. W., Willett P. Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques. FEBS Letters. 303:1992;48-52.
    • (1992) FEBS Letters , vol.303 , pp. 48-52
    • Artymiuk, P.J.1    Grindley, H.M.2    Park, J.E.3    Rice, D.W.4    Willett, P.5
  • 6
    • 0026758369 scopus 로고
    • Cloning, characterization, and expression of the dapE gene of Escherichia coli
    • Bouvier J., Richaud C., Higgins W., Bogler O., Stragier P. Cloning, characterization, and expression of the dapE gene of Escherichia coli. J. Bacteriol. 174:1992;5265-5271.
    • (1992) J. Bacteriol. , vol.174 , pp. 5265-5271
    • Bouvier, J.1    Richaud, C.2    Higgins, W.3    Bogler, O.4    Stragier, P.5
  • 7
    • 0026691392 scopus 로고
    • Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related
    • Boyen A., Charlier D., Charlier J., Sakanyan V., Mett I., Glansdorff N. Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related. Gene. 116:1992;1-6.
    • (1992) Gene , vol.116 , pp. 1-6
    • Boyen, A.1    Charlier, D.2    Charlier, J.3    Sakanyan, V.4    Mett, I.5    Glansdorff, N.6
  • 8
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier B., Schalk C., D'Orchymont H., Rondeau J. M., Moras D., Tarnus C. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure. 2:1994;283-291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.M.4    Moras, D.5    Tarnus, C.6
  • 10
    • 0000596754 scopus 로고
    • Mechanism of carboxypeptidase A: Hydration of a ketonic substrate analogue
    • Christianson D. W., David P. R., Lipscomb W. N. Mechanism of carboxypeptidase A: hydration of a ketonic substrate analogue. Proc. Natl Acad. Sci. USA. 84:1987;1512-1515.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1512-1515
    • Christianson, D.W.1    David, P.R.2    Lipscomb, W.N.3
  • 11
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15:1997;133-138.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 133-138
    • Esnouf, R.1
  • 12
    • 0029901637 scopus 로고    scopus 로고
    • Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods
    • Felsenstein J. Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods. Methods Enzymol. 266:1996;418-427.
    • (1996) Methods Enzymol. , vol.266 , pp. 418-427
    • Felsenstein, J.1
  • 13
    • 0040974381 scopus 로고    scopus 로고
    • The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen
    • Garcia-Saez I., Reverter D., Vendrell J., Aviles F. X., Coll M. The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. EMBO J. 16:1997;6906-6913.
    • (1997) EMBO J. , vol.16 , pp. 6906-6913
    • Garcia-Saez, I.1    Reverter, D.2    Vendrell, J.3    Aviles, F.X.4    Coll, M.5
  • 14
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 15
    • 0027271928 scopus 로고
    • Characterization of the sporulation-related gamma- D -glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein
    • Hourdou M. L., Guinand M., Vacheron M. J., Michel G., Denoroy L., Duez C., Englebert S., Joris B., Weber G., Ghuysen J. M. Characterization of the sporulation-related gamma- D -glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein. Biochem. J. 292:1993;563-570.
    • (1993) Biochem. J. , vol.292 , pp. 563-570
    • Hourdou, M.L.1    Guinand, M.2    Vacheron, M.J.3    Michel, G.4    Denoroy, L.5    Duez, C.6    Englebert, S.7    Joris, B.8    Weber, G.9    Ghuysen, J.M.10
  • 16
    • 0030690922 scopus 로고    scopus 로고
    • Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway inPseudomonas aeruginosa
    • Itoh Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway inPseudomonas aeruginosa. J. Bacteriol. 179:1997;7280-7290.
    • (1997) J. Bacteriol. , vol.179 , pp. 7280-7290
    • Itoh, Y.1
  • 17
    • 0027362434 scopus 로고
    • Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease
    • Kaul R., Gao G. P., Balamurugan K., Matalon R. Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease. Nature Genet. 5:1993;118-123.
    • (1993) Nature Genet. , vol.5 , pp. 118-123
    • Kaul, R.1    Gao, G.P.2    Balamurugan, K.3    Matalon, R.4
  • 18
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots structures
    • Kraulis P. Molscript: a program to produce both detailed and schematic plots structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 20
    • 0032104477 scopus 로고    scopus 로고
    • How far divergent evolution goes in proteins
    • Murzin A. G. How far divergent evolution goes in proteins. Curr. Opin. Struct. Biol. 8:1998;380-387.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 380-387
    • Murzin, A.G.1
  • 21
    • 0030581683 scopus 로고    scopus 로고
    • A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line
    • Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K., Okubo K. A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line. Biochem. Biophys. Res. Commun. 228:1996;411-414.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 411-414
    • Ohno, I.1    Hashimoto, J.2    Shimizu, K.3    Takaoka, K.4    Ochi, T.5    Matsubara, K.6    Okubo, K.7
  • 23
    • 0029994544 scopus 로고    scopus 로고
    • Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1
    • Phillips M. A., Rutter W. J. Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1. Biochemistry. 35:1996;6771-6776.
    • (1996) Biochemistry , vol.35 , pp. 6771-6776
    • Phillips, M.A.1    Rutter, W.J.2
  • 24
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings N. D., Barrett A. J. Evolutionary families of metallopeptidases. Methods Enzymol. 248:1995;183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 25
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Funct. Genet. 19:1994;55-72.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 26
    • 0031569353 scopus 로고    scopus 로고
    • Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy
    • Rowsell S., Pauptit R. A., Tucker A. D., Melton R. G., Blow D. M., Brick P. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure. 5:1997;337-347.
    • (1997) Structure , vol.5 , pp. 337-347
    • Rowsell, S.1    Pauptit, R.A.2    Tucker, A.D.3    Melton, R.G.4    Blow, D.M.5    Brick, P.6
  • 27
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three- dimensional side-chain patterns: New examples of convergent evolution
    • Russell R. B. Detection of protein three- dimensional side-chain patterns: new examples of convergent evolution. J. Mol. Biol. 279:1998;1211-1227.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1211-1227
    • Russell, R.B.1
  • 28
    • 0031827017 scopus 로고    scopus 로고
    • Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli
    • Schneider B. L., Kiupakis A. K., Reitzer L. J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180:1998;4278-4286.
    • (1998) J. Bacteriol. , vol.180 , pp. 4278-4286
    • Schneider, B.L.1    Kiupakis, A.K.2    Reitzer, L.J.3
  • 29
    • 0029364939 scopus 로고
    • Multiple alignment of biopolymer sequences, based on the search for statistically significant common segments
    • Seledtsov I. A., Vul'f Iu. I., Makarova K. S. Multiple alignment of biopolymer sequences, based on the search for statistically significant common segments. Mol. Biol. (Mosk.). 29:1995;1023-1039.
    • (1995) Mol. Biol. (Mosk.) , vol.29 , pp. 1023-1039
    • Seledtsov, I.A.1    Vul'F, Iu.i.2    Makarova, K.S.3
  • 30
    • 0030888061 scopus 로고    scopus 로고
    • Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase
    • Song L., Fricker L. D. Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase. J. Biol. Chem. 272:1997;10543-10550.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10543-10550
    • Song, L.1    Fricker, L.D.2
  • 31
    • 0029006137 scopus 로고
    • Carboxypeptidase T
    • Stepanov V. M. Carboxypeptidase T. Methods Enzymol. 248:1995;675-683.
    • (1995) Methods Enzymol. , vol.248 , pp. 675-683
    • Stepanov, V.M.1
  • 32
    • 0004053611 scopus 로고
    • Brisbane, Toronto, Singapore: John Wiley & Sons, Inc., New York, Chichester
    • Voet D., Voet J. G. Biochemistry. 1990;John Wiley & Sons, Inc., New York, Chichester, Brisbane, Toronto, Singapore.
    • (1990) Biochemistry
    • Voet, D.1    Voet, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.