메뉴 건너뛰기




Volumn 182, Issue 9, 2000, Pages 2536-2543

Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

MICROSOMAL AMINOPEPTIDASE; SERINE DEHYDRATASE;

EID: 0033994940     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.9.2536-2543.2000     Document Type: Article
Times cited : (20)

References (19)
  • 2
    • 0024789654 scopus 로고
    • Superpolylinkers in cloning and expression vectors
    • Brosius, J. 1989. Superpolylinkers in cloning and expression vectors. DNA 8:759-777.
    • (1989) DNA , vol.8 , pp. 759-777
    • Brosius, J.1
  • 4
    • 0342884296 scopus 로고
    • Ph.D. thesis. Case Western Reserve University, Cleveland, Ohio
    • Carter, T. H. 1982. Ph.D. thesis. Case Western Reserve University, Cleveland, Ohio.
    • (1982)
    • Carter, T.H.1
  • 5
    • 0021176041 scopus 로고
    • Aspartate-specific peptidases in Salmonella typhimurium: Mutants deficient in peptidase
    • Carter, T. H., and C. G. Miller. 1984. Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E. J. Bacteriol. 159:453-459.
    • (1984) E. J. Bacteriol. , vol.159 , pp. 453-459
    • Carter, T.H.1    Miller, C.G.2
  • 6
    • 0028158127 scopus 로고
    • Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an α-aspartyl dipeptidase
    • Conlin, C. A., K. Håkansson, A. Liljas, and C. G. Miller. 1994. Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an α-aspartyl dipeptidase. J. Bacteriol. 176:166-172.
    • (1994) J. Bacteriol. , vol.176 , pp. 166-172
    • Conlin, C.A.1    Håkansson, K.2    Liljas, A.3    Miller, C.G.4
  • 7
    • 0024393375 scopus 로고
    • Introduction of a cysteine protease active site into trypsin
    • Higaki, J. N., L. B. Evnin, and C. S. Craik. 1989. Introduction of a cysteine protease active site into trypsin. Biochemistry 28:9256-9263.
    • (1989) Biochemistry , vol.28 , pp. 9256-9263
    • Higaki, J.N.1    Evnin, L.B.2    Craik, C.S.3
  • 9
    • 0028841887 scopus 로고
    • Identification of active site residues of the Tsp protease
    • Keiler, K. C., and R. T. Sauer. 1995. Identification of active site residues of the Tsp protease. J. Biol. Chem. 270:28864-28868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28864-28868
    • Keiler, K.C.1    Sauer, R.T.2
  • 11
    • 0016251715 scopus 로고
    • Isolation and characterization of proline peptidase mutants of Salmonella typhimurium
    • McHugh, G. L., and C. G. Miller. 1974. Isolation and characterization of proline peptidase mutants of Salmonella typhimurium. J. Bacteriol. 120:364-371.
    • (1974) J. Bacteriol. , vol.120 , pp. 364-371
    • McHugh, G.L.1    Miller, C.G.2
  • 12
    • 0000661488 scopus 로고    scopus 로고
    • Protein degradation and proteolytic modification
    • In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Miller, C. G. 1996. Protein degradation and proteolytic modification, p. 938-954. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 938-954
    • Miller, C.G.1
  • 13
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings, N. D., and A. J. Barrett. 1993. Evolutionary families of peptidases. Biochem. J. 290:205-218.
    • (1993) Biochem. J. , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 14
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 15
    • 0015449701 scopus 로고
    • Phage P22 mutants with increased or decreased transduction abilities
    • Schmieger, H. 1972. Phage P22 mutants with increased or decreased transduction abilities. Mol. Gen. Genet. 119:75-88.
    • (1972) Mol. Gen. Genet. , vol.119 , pp. 75-88
    • Schmieger, H.1
  • 16
    • 0025108763 scopus 로고
    • Substrate specificity of the protease that processes human interleukin-1 beta
    • Sleath, P. R., R. C. Hendrickson, S. R. Kronheim, C. J. March, and R. A. Black. 1990. Substrate specificity of the protease that processes human interleukin-1 beta. J. Biol. Chem. 265:14526-14528.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14526-14528
    • Sleath, P.R.1    Hendrickson, R.C.2    Kronheim, S.R.3    March, C.J.4    Black, R.A.5
  • 17
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel, H. J., and D. M. Bonner. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 18
    • 0027220692 scopus 로고
    • Thyroid hormone-induced gene expression program for amphibian tail resorption
    • Wang, Z., and D. D. Brown. 1993. Thyroid hormone-induced gene expression program for amphibian tail resorption. J. Biol. Chem. 268:16270-16278.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16270-16278
    • Wang, Z.1    Brown, D.D.2
  • 19
    • 0019139986 scopus 로고
    • Peptide accumulation during growth of peptidase deficient mutants
    • Yen, C., L. Green, and C. G. Miller. 1980. Peptide accumulation during growth of peptidase deficient mutants. J. Mol. Biol. 143:35-48.
    • (1980) J. Mol. Biol. , vol.143 , pp. 35-48
    • Yen, C.1    Green, L.2    Miller, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.