메뉴 건너뛰기




Volumn 1, Issue , 2004, Pages 868-871

Pitrilysin

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84944031869     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50266-4     Document Type: Chapter
Times cited : (3)

References (19)
  • 1
    • 0028879135 scopus 로고
    • Role of yeast in insulin-degrading enzyme homologs in propheromone processing and bud site selection
    • N. Adames, K. Blundell, M.N. Ashby and C. Boone (1995) Role of yeast in insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270 464-467.
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 2
    • 0024215473 scopus 로고
    • Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III
    • J.A. Affholter, V.A. Fried and R.A. Roth (1988) Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242 1415-1418.
    • (1988) Science , vol.242 , pp. 1415-1418
    • Affholter, J.A.1    Fried, V.A.2    Roth, R.A.3
  • 4
    • 0027411475 scopus 로고
    • Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay
    • A. Anastasi, C.G. Knight and A.J. Barrett (1993) Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay. Biochem. J. 290 601-607.
    • (1993) Biochem. J. , vol.290 , pp. 601-607
    • Anastasi, A.1    Knight, C.G.2    Barrett, A.J.3
  • 5
    • 0025855940 scopus 로고
    • Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo
    • F. Baneyx and G. Georgiou (1991) Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo. J. Bacteriol. 173 2696-2703.
    • (1991) J. Bacteriol. , vol.173 , pp. 2696-2703
    • Baneyx, F.1    Georgiou, G.2
  • 6
    • 0026516458 scopus 로고
    • An unusual active site identified in a family of zinc metalloendopeptidases
    • A.B. Becker and R.A. Roth (1992) An unusual active site identified in a family of zinc metalloendopeptidases. Proc. Natl. Acad. Sci. USA 89 3835-3839.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3835-3839
    • Becker, A.B.1    Roth, R.A.2
  • 7
    • 0027263747 scopus 로고
    • Identification of glutamate 169 as the third zinc binding residue in protease III, a member of the family of insulin-degrading enzymes
    • A.B. Becker and R.A. Roth (1993) Identification of glutamate 169 as the third zinc binding residue in protease III, a member of the family of insulin-degrading enzymes. Biochem. J. 292 137-142.
    • (1993) Biochem. J. , vol.292 , pp. 137-142
    • Becker, A.B.1    Roth, R.A.2
  • 8
    • 0029022718 scopus 로고
    • Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria
    • A.B. Becker and R.A. Roth (1995) Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria. Methods Enzymol. 248 693-703.
    • (1995) Methods Enzymol. , vol.248 , pp. 693-703
    • Becker, A.B.1    Roth, R.A.2
  • 9
    • 0018379064 scopus 로고
    • Purification and characterization of protease III from Escherichia coli
    • Y.-S. Cheng and D. Zipser (1979) Purification and characterization of protease III from Escherichia coli. J. Biol. Chem. 254 4698-4706.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4698-4706
    • Cheng, Y.-S.1    Zipser, D.2
  • 10
    • 0026800773 scopus 로고
    • Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III
    • L. Ding, A.B. Becker, A. Suzuki and R.A. Roth (1992) Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. J. Biol. Chem. 267 2414-2420.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2414-2420
    • Ding, L.1    Becker, A.B.2    Suzuki, A.3    Roth, R.A.4
  • 11
    • 0021350640 scopus 로고
    • Physical and biochemical analysis of the cloned recB and recC genes of Escherichia coli K-12
    • C. Dykstra, D. Prasher and S. Kushner (1984) Physical and biochemical analysis of the cloned recB and recC genes of Escherichia coli K-12. J. Bacteriol. 157 21-27.
    • (1984) J. Bacteriol. , vol.157 , pp. 21-27
    • Dykstra, C.1    Prasher, D.2    Kushner, S.3
  • 12
    • 0023046298 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III
    • P.W. Finch, R.E. Wilson, K. Brown, I.D. Hickson and P.T. Emmerson (1986) Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III. Nucleic Acids Res. 14 7695-7703.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7695-7703
    • Finch, P.W.1    Wilson, R.E.2    Brown, K.3    Hickson, I.D.4    Emmerson, P.T.5
  • 13
    • 0028151340 scopus 로고
    • A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes
    • A. Fujita, C. Oka, Y. Arikawa, T. Katagai, A. Tonouchi, S. Kuhara and Y. Misumi (1994) A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature 372 567-570.
    • (1994) Nature , vol.372 , pp. 567-570
    • Fujita, A.1    Oka, C.2    Arikawa, Y.3    Katagai, T.4    Tonouchi, A.5    Kuhara, S.6    Misumi, Y.7
  • 14
    • 0011021887 scopus 로고
    • Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli
    • K.I. Kim, S.H. Baek, Y.-M. Hong, M.-S. Kang, D.B. Ha, A.L. Goldberg and C.H. Chung (1995) Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli. J. Biol. Chem. 270 29799-29805.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29799-29805
    • Kim, K.I.1    Baek, S.H.2    Hong, Y.-M.3    Kang, M.-S.4    Ha, D.B.5    Goldberg, A.L.6    Chung, C.H.7
  • 16
    • 0025828357 scopus 로고
    • Homologues of insulinase, a new superfamily of metalloendopeptidases
    • N.D. Rawlings and A.J. Barrett (1991) Homologues of insulinase, a new superfamily of metalloendopeptidases. Biochem. J. 275 389-391.
    • (1991) Biochem. J. , vol.275 , pp. 389-391
    • Rawlings, N.D.1    Barrett, A.J.2
  • 17
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • N.D. Rawlings and A.J. Barrett (1995) Evolutionary families of metallopeptidases. Methods Enzymol. 248 183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 18
    • 0019862897 scopus 로고
    • E. coli contains eight soluble proteolytic activities, one being ATP-dependent
    • K.H.S. Swamy and A.L. Goldberg (1981) E. coli contains eight soluble proteolytic activities, one being ATP-dependent. Nature 292 652-654.
    • (1981) Nature , vol.292 , pp. 652-654
    • Swamy, K.H.S.1    Goldberg, A.L.2
  • 19
    • 0020079743 scopus 로고
    • Subcellular distribution of various proteases in Escherichia coli
    • K.H.S. Swamy and A.L. Goldberg (1982) Subcellular distribution of various proteases in Escherichia coli. J. Bacteriol. 149 1027-1033.
    • (1982) J. Bacteriol. , vol.149 , pp. 1027-1033
    • Swamy, K.H.S.1    Goldberg, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.