메뉴 건너뛰기




Volumn 120, Issue 3, 1996, Pages 564-572

Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22

Author keywords

Acid proteinase; Carboxyl proteinase; Cloning; Pepstatin; Xanthomonas

Indexed keywords

ACID PROTEINASE; BACTERIAL ENZYME; ENZYME PRECURSOR; PEPSTATIN; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN;

EID: 0029761009     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021451     Document Type: Article
Times cited : (49)

References (58)
  • 1
    • 0003755878 scopus 로고
    • Aspartic proteinases and their inhibitors
    • Kostka, V., ed. Walter de Gruyter, Berlin
    • Kay, J. (1985) Aspartic proteinases and their inhibitors in Aspartic Proteinases and Their Inhibitors (Kostka, V., ed.) pp. 1 17, Walter de Gruyter, Berlin
    • (1985) Aspartic Proteinases and Their Inhibitors , pp. 117
    • Kay, J.1
  • 2
    • 0006097121 scopus 로고
    • Pepstatin-insensitive acid proteinases
    • Kostka, V., ed. Walter de Gruyter, Berlin
    • Murao, S. and Oda, K. (1985) Pepstatin-insensitive acid proteinases in Aspartic Proteinases and Their Inhibitors (Kostka, V., ed.) pp. 379-399, Walter de Gruyter, Berlin
    • (1985) Aspartic Proteinases and Their Inhibitors , pp. 379-399
    • Murao, S.1    Oda, K.2
  • 6
    • 0001464924 scopus 로고
    • New pepsin inhibitors (S-PI) from Streptomyces EF-44-201
    • Murao, S. and Satoi, S. (1970) New pepsin inhibitors (S-PI) from Streptomyces EF-44-201. Agric. Biol. Chem. 34, 1265-1267
    • (1970) Agric. Biol. Chem. , vol.34 , pp. 1265-1267
    • Murao, S.1    Satoi, S.2
  • 7
    • 0014027980 scopus 로고
    • The inactivation of pepsin by diazoacetyl-norleucine methyl ester
    • Rajagopalan, T.G., Stein, W.H., and Moore, S. (1966) The inactivation of pepsin by diazoacetyl-norleucine methyl ester. J. Biol. Chem. 241, 4295-4297
    • (1966) J. Biol. Chem. , vol.241 , pp. 4295-4297
    • Rajagopalan, T.G.1    Stein, W.H.2    Moore, S.3
  • 8
    • 0015239836 scopus 로고
    • Specific and irreversible inactivation of pepsin by substrate-like epoxides
    • Tang, J. (1971) Specific and irreversible inactivation of pepsin by substrate-like epoxides. J. Biol. Chem. 246, 4510-4517
    • (1971) J. Biol. Chem. , vol.246 , pp. 4510-4517
    • Tang, J.1
  • 10
    • 0023644546 scopus 로고
    • Amino acid sequence of rhizopuspepsin isozyme pI 5
    • Delaney, R., Wong, R.N.S., Meng, G., Wu, N., and Tang, J. (1987) Amino acid sequence of rhizopuspepsin isozyme pI 5. J. Biol. Chem. 262, 1461-1467
    • (1987) J. Biol. Chem. , vol.262 , pp. 1461-1467
    • Delaney, R.1    Wong, R.N.S.2    Meng, G.3    Wu, N.4    Tang, J.5
  • 11
    • 84954976476 scopus 로고
    • New acid proteases from Scytalidium lignicolum M-133
    • Murao, S., Oda, K., and Matsushita, Y. (1972) New acid proteases from Scytalidium lignicolum M-133. Agric. Biol. Chem. 36, 1647-1650
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1647-1650
    • Murao, S.1    Oda, K.2    Matsushita, Y.3
  • 12
    • 84998498632 scopus 로고
    • Isolation and identification of a microorganism which produces non Streptomyces pepsin inhibitor and N-diazoacetyl-DL-norleucine methylester sensitive acid proteases
    • Murao, S., Oda, K., and Matsushita, Y. (1973) Isolation and identification of a microorganism which produces non Streptomyces pepsin inhibitor and N-diazoacetyl-DL-norleucine methylester sensitive acid proteases. Agric. Biol. Chem. 37, 1417-1421
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1417-1421
    • Murao, S.1    Oda, K.2    Matsushita, Y.3
  • 13
    • 0016153960 scopus 로고
    • Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568
    • Oda, K. and Murao, S. (1974) Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 38, 2435-2444
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 2435-2444
    • Oda, K.1    Murao, S.2
  • 14
    • 0000954429 scopus 로고
    • Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568
    • Oda, K., Torishima, H., and Murao, S. (1986) Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 50, 651-658
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 651-658
    • Oda, K.1    Torishima, H.2    Murao, S.3
  • 15
    • 0007932957 scopus 로고
    • Some physicochemical properties and substrate specificity of acid protease B of Scytalidium lignicolum ATCC 24568
    • Oda, K., Murao, S., Oka, T., and Morihara, K. (1975) Some physicochemical properties and substrate specificity of acid protease B of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 39, 477-484
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 477-484
    • Oda, K.1    Murao, S.2    Oka, T.3    Morihara, K.4
  • 16
    • 0007924467 scopus 로고
    • Some physicochemical properties and substrate specificities of acid protease A-1 and A-2 of Scytalidium lignicolumn ATCC 24568
    • Oda, K., Murao, S., Oka, T., and Morihara, K. (1976) Some physicochemical properties and substrate specificities of acid protease A-1 and A-2 of Scytalidium lignicolumn ATCC 24568. Agric. Biol. Chem. 40, 859-866
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 859-866
    • Oda, K.1    Murao, S.2    Oka, T.3    Morihara, K.4
  • 17
    • 0018452208 scopus 로고
    • Pepstatin-insensitive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides
    • Morihara, K., Tsuzuki, H., Murao, S., and Oda, K. (1979) Pepstatin-insensitive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. J. Biochem. 85, 661-668
    • (1979) J. Biochem. , vol.85 , pp. 661-668
    • Morihara, K.1    Tsuzuki, H.2    Murao, S.3    Oda, K.4
  • 18
    • 0345541896 scopus 로고
    • Comparative specificity of microbial acid proteinases
    • Turk, V. and Vitale, L.J., eds. Mladinska Knjiga-Pergamon Press, Ljubljana, Oxford
    • Morihara, K. (1981) Comparative specificity of microbial acid proteinases in Proteinases and Their Inhibitors: Structure, Function, and Applied Aspects (Turk, V. and Vitale, L.J., eds.) pp. 213-222, Mladinska Knjiga-Pergamon Press, Ljubljana, Oxford
    • (1981) Proteinases and Their Inhibitors: Structure, Function, and Applied Aspects , pp. 213-222
    • Morihara, K.1
  • 19
    • 0007877133 scopus 로고
    • Action of Scytalidium lignicolum acid proteases on insulin B-chain
    • Oda, K. and Murao, S. (1976) Action of Scytalidium lignicolum acid proteases on insulin B-chain. Agric. Biol. Chem. 40, 1221-1225
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 1221-1225
    • Oda, K.1    Murao, S.2
  • 20
    • 85004455867 scopus 로고
    • Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate
    • Majima, E., Oda, K., Murao, S., and Ichishima, E. (1988) Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate. Agric. Biol. Chem. 52, 787-793
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 787-793
    • Majima, E.1    Oda, K.2    Murao, S.3    Ichishima, E.4
  • 21
  • 22
    • 0022497308 scopus 로고
    • Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B
    • Tsuru, D., Shimada, S., Maruta, S., Yoshimoto, T., Oda, K., Murao, S., Miyata, T., and Iwanaga, S. (1986) Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B. J. Biochem. 99, 1537-1539
    • (1986) J. Biochem. , vol.99 , pp. 1537-1539
    • Tsuru, D.1    Shimada, S.2    Maruta, S.3    Yoshimoto, T.4    Oda, K.5    Murao, S.6    Miyata, T.7    Iwanaga, S.8
  • 23
    • 0024818436 scopus 로고
    • Inactivation of Scytalidium lignicolum acid protease B with 1,2-epoxy-3-(4′-azido-2′-nitrophenoxy)propane
    • Tsuru, D., Naotsuka, A., Kobayashi, R., Yoshimoto, T., Oda, K., and Murao, S. (1989) Inactivation of Scytalidium lignicolum acid protease B with 1,2-epoxy-3-(4′-azido-2′-nitrophenoxy)propane. Agric. Biol. Chem. 53, 2751-2756
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2751-2756
    • Tsuru, D.1    Naotsuka, A.2    Kobayashi, R.3    Yoshimoto, T.4    Oda, K.5    Murao, S.6
  • 24
    • 0008191626 scopus 로고
    • Inhibition of Scytalidium lignicolum acid protease B by 1-diazo-3-phenyl-2-propanone
    • Tsuru, D., Kobayashi, R., Nakagawa, N., and Yoshimoto, T. (1989) Inhibition of Scytalidium lignicolum acid protease B by 1-diazo-3-phenyl-2-propanone. Agric. Biol. Chem. 53, 1305-1312
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 1305-1312
    • Tsuru, D.1    Kobayashi, R.2    Nakagawa, N.3    Yoshimoto, T.4
  • 25
    • 0017042829 scopus 로고
    • Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus
    • Chang, W.J., Horiuchi, S., Takahashi, K., Yamasaki, M., and Yamada, Y. (1976) Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus. J. Biochem. 80, 975-981
    • (1976) J. Biochem. , vol.80 , pp. 975-981
    • Chang, W.J.1    Horiuchi, S.2    Takahashi, K.3    Yamasaki, M.4    Yamada, Y.5
  • 26
    • 0007876427 scopus 로고
    • Occurrence of Streptomyces pepsin inhibitor-insensitive carboxyl proteinase in Basidiomycetes. Agric
    • Oda, K., Terashita, T., Kono, M., and Murao, S. (1981) Occurrence of Streptomyces pepsin inhibitor-insensitive carboxyl proteinase in Basidiomycetes. Agric. Biol. Chem. 45, 2339-2340
    • (1981) Biol. Chem. , vol.45 , pp. 2339-2340
    • Oda, K.1    Terashita, T.2    Kono, M.3    Murao, S.4
  • 27
    • 84953967145 scopus 로고
    • Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Lentinus edodes
    • Terashita, T., Oda, K., Kono, M., and Murao, S. (1981) Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Lentinus edodes. Agric. Biol. Chem. 45, 1937-1943
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 1937-1943
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 28
    • 84953965833 scopus 로고
    • Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum
    • Terashita, T., Oda, K., Kono, M., and Murao, S. (1984) Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum. Agric. Biol. Chem. 48, 1029-1035
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1029-1035
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 29
    • 0007877365 scopus 로고
    • Purification and characterization of pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus)
    • Kobayashi, H., Kusakabe, I., and Murakami, K. (1985) Purification and characterization of pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus). Agric. Biol. Chem. 49, 2393-2397
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2393-2397
    • Kobayashi, H.1    Kusakabe, I.2    Murakami, K.3
  • 30
    • 0023154620 scopus 로고
    • Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium
    • Oda, K., Sugutani, M., Fukuhara, K., and Murao, S. (1987) Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium. Biochim. Biophys. Acta 923, 463-469
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 463-469
    • Oda, K.1    Sugutani, M.2    Fukuhara, K.3    Murao, S.4
  • 31
    • 85010093042 scopus 로고
    • Purification and properties of an S-PI (pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium
    • Oda, K., Nakazima, T., Terashita, T., Suzuki, K., and Murao, S. (1987) Purification and properties of an S-PI (pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium. Agric. Biol. Chem. 51, 3073-3080
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 3073-3080
    • Oda, K.1    Nakazima, T.2    Terashita, T.3    Suzuki, K.4    Murao, S.5
  • 32
    • 0000077693 scopus 로고
    • A novel thermostable, S-PI (pepstatin Ac)-insensitive acid proteinase from thermophilic Bacillus novosp. strain MN-32
    • Murao, S., Ohkuni, K., Nagao, M., Oda, K., and Shin, T. (1988) A novel thermostable, S-PI (pepstatin Ac)-insensitive acid proteinase from thermophilic Bacillus novosp. strain MN-32. Agric. Biol. Chem. 52, 1629-1631
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1629-1631
    • Murao, S.1    Ohkuni, K.2    Nagao, M.3    Oda, K.4    Shin, T.5
  • 33
    • 0027446449 scopus 로고
    • Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32
    • Murao, S., Ohkuni, K., Nagao, M., Hirayama, K., Fukuhara, K., Oda, K., Oyama, H., and Shin, T. (1993) Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32. J. Biol. Chem. 268, 349-355
    • (1993) J. Biol. Chem. , vol.268 , pp. 349-355
    • Murao, S.1    Ohkuni, K.2    Nagao, M.3    Hirayama, K.4    Fukuhara, K.5    Oda, K.6    Oyama, H.7    Shin, T.8
  • 34
    • 0029002927 scopus 로고
    • A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp
    • Toogood, H.S., Prescott, M., and Daniel, R.M. (1995) A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp. Biochem. J. 307, 783-789
    • (1995) Biochem. J. , vol.307 , pp. 783-789
    • Toogood, H.S.1    Prescott, M.2    Daniel, R.M.3
  • 35
    • 0000916308 scopus 로고
    • A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases
    • Oda, K., Fukuda, Y., Murao, S., Uchida, K., and Kainosho, M. (1989) A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases. Agric. Biol. Chem. 53, 405-415
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 405-415
    • Oda, K.1    Fukuda, Y.2    Murao, S.3    Uchida, K.4    Kainosho, M.5
  • 36
    • 0028815656 scopus 로고
    • The primary structure of pepstatin-insensitive carboxyl proteinase produced by Pseudomonas sp. No. 101
    • Hayashi, K., Izu, H., Oda, K., Fukuhara, K., Matsuo, M., Takano, R., and Hara, S. (1995) The primary structure of pepstatin-insensitive carboxyl proteinase produced by Pseudomonas sp. No. 101. J. Biochem. 118, 738-744
    • (1995) J. Biochem. , vol.118 , pp. 738-744
    • Hayashi, K.1    Izu, H.2    Oda, K.3    Fukuhara, K.4    Matsuo, M.5    Takano, R.6    Hara, S.7
  • 37
    • 0016740676 scopus 로고
    • Studies on the interaction between Streptomyces pepsin inhibitor and several acid proteinases by means of a zinc(II)-dye complex as a probe
    • Nakatani, H., Hiromi, K., Satoi, S., Oda, K., Murao, S., and Ichishima, E. (1975) Studies on the interaction between Streptomyces pepsin inhibitor and several acid proteinases by means of a zinc(II)-dye complex as a probe. Biochim. Biophys. Acta 391, 415-421
    • (1975) Biochim. Biophys. Acta , vol.391 , pp. 415-421
    • Nakatani, H.1    Hiromi, K.2    Satoi, S.3    Oda, K.4    Murao, S.5    Ichishima, E.6
  • 38
    • 0026555406 scopus 로고
    • Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101
    • Oda, K., Nakatani, H., and Dunn, B.M. (1992) Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101. Biochim. Biophys. Acta 1120, 208-214
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 208-214
    • Oda, K.1    Nakatani, H.2    Dunn, B.M.3
  • 39
    • 0028046586 scopus 로고
    • Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101
    • Oda, K., Takahashi, T., Tokuda, Y., Shibano, Y., and Takahashi, S. (1994) Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101. J. Biol. Chem. 269, 26518-26524
    • (1994) J. Biol. Chem. , vol.269 , pp. 26518-26524
    • Oda, K.1    Takahashi, T.2    Tokuda, Y.3    Shibano, Y.4    Takahashi, S.5
  • 40
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 41
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. (1961) A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3, 208-218
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 42
    • 0009482260 scopus 로고
    • Electrophretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 44
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E.M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98, 503-517
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 45
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J. and Dalgarno, L. (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71, 1342-1346
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 46
    • 0025090011 scopus 로고
    • A multipurpose broad host range cloning vector and its use to characterise an extracellular protease gene of Xanthomonas campestris pathovar campestris
    • Liu, Y.-N., Tang, J.-L., Clarke, B.R., Dow, J.M., and Daniels, M.J. (1990) A multipurpose broad host range cloning vector and its use to characterise an extracellular protease gene of Xanthomonas campestris pathovar campestris. Mol. Gen. Genet. 220, 433-440
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 433-440
    • Liu, Y.-N.1    Tang, J.-L.2    Clarke, B.R.3    Dow, J.M.4    Daniels, M.J.5
  • 48
    • 0027397655 scopus 로고
    • Cloning and characterization of the glutamate 1-semialdehyde aminomutase gene from Xanthomonas campestris pv. phaseoli
    • Murakami, K., Korbsrisate, S., Asahara, N., Hashimoto, Y., and Murooka, Y. (1993) Cloning and characterization of the glutamate 1-semialdehyde aminomutase gene from Xanthomonas campestris pv. phaseoli. Appl. Microbiol. Biotechnol. 38, 502-506
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 502-506
    • Murakami, K.1    Korbsrisate, S.2    Asahara, N.3    Hashimoto, Y.4    Murooka, Y.5
  • 49
    • 0027401283 scopus 로고
    • Restoration of pathogenicity of avirulent Xanthomonas oryzae pv. oryzae and X. campestris pathovars by reciprocal complementation with the hrpXo and hrpXc genes and identification of HrpX function by sequence analyses
    • Kamdar, H.V., Kamoun, S., and Kado, C.I. (1993) Restoration of pathogenicity of avirulent Xanthomonas oryzae pv. oryzae and X. campestris pathovars by reciprocal complementation with the hrpXo and hrpXc genes and identification of HrpX function by sequence analyses. J. Bacteriol. 175, 2017-2025
    • (1993) J. Bacteriol. , vol.175 , pp. 2017-2025
    • Kamdar, H.V.1    Kamoun, S.2    Kado, C.I.3
  • 51
    • 0024351627 scopus 로고
    • Cloning, nucleotide sequence, and expression of Achromobacter protease I gene
    • Ohara, T., Makino, K., Shinagawa, H., Nakata, A., Norioka, S., and Sakiyama, F. (1989) Cloning, nucleotide sequence, and expression of Achromobacter protease I gene. J. Biol. Chem. 264, 20625-20631
    • (1989) J. Biol. Chem. , vol.264 , pp. 20625-20631
    • Ohara, T.1    Makino, K.2    Shinagawa, H.3    Nakata, A.4    Norioka, S.5    Sakiyama, F.6
  • 52
    • 0027732836 scopus 로고
    • Cloning and sequence of an alkaline serine protease-encoding gene from the marine bacterium Alteromonas sp. strain 0-7
    • Tsujibo, H., Miyamoto, K., Tanaka, K., Kawai, M., Tainaka, K., Imada, C., Okami, Y., and Inamori, Y. (1993) Cloning and sequence of an alkaline serine protease-encoding gene from the marine bacterium Alteromonas sp. strain 0-7. Gene 136, 247-251
    • (1993) Gene , vol.136 , pp. 247-251
    • Tsujibo, H.1    Miyamoto, K.2    Tanaka, K.3    Kawai, M.4    Tainaka, K.5    Imada, C.6    Okami, Y.7    Inamori, Y.8
  • 53
    • 0026538941 scopus 로고
    • Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus
    • David, V.A., Deutch, A.H., Sloma, A., Pawlyk, D., Ally, A., and Durham, D.R. (1992) Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. Gene 112, 107-112
    • (1992) Gene , vol.112 , pp. 107-112
    • David, V.A.1    Deutch, A.H.2    Sloma, A.3    Pawlyk, D.4    Ally, A.5    Durham, D.R.6
  • 54
    • 0024519951 scopus 로고
    • Nucleotide sequence of the Vibrio alginolyticus calcium-dependent, detergent-resistant alkaline serine exoprotease A
    • Deane, S.M., Robb, F.T., Robb, S.M., and Woods, D.R. (1989) Nucleotide sequence of the Vibrio alginolyticus calcium-dependent, detergent-resistant alkaline serine exoprotease A. Gene 76, 281-288
    • (1989) Gene , vol.76 , pp. 281-288
    • Deane, S.M.1    Robb, F.T.2    Robb, S.M.3    Woods, D.R.4
  • 55
    • 0028360863 scopus 로고
    • Requirement of a COOH-terminal pro-sequence for the extracellular secretion of aqualysin I (a thermophilic subtilisin-type protease) in Thermus thermophilus
    • Lee, Y.-C., Koike, H., Taguchi, H., Ohta, T., and Matsuzawa, H. (1994) Requirement of a COOH-terminal pro-sequence for the extracellular secretion of aqualysin I (a thermophilic subtilisin-type protease) in Thermus thermophilus. FEMS Microbiol. Lett. 120, 69-74
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 69-74
    • Lee, Y.-C.1    Koike, H.2    Taguchi, H.3    Ohta, T.4    Matsuzawa, H.5
  • 56
    • 0022652268 scopus 로고
    • Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli
    • Yanagida, N., Uozumi, T., and Beppu, T. (1986) Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli. J. Bacteriol. 166, 937-944
    • (1986) J. Bacteriol. , vol.166 , pp. 937-944
    • Yanagida, N.1    Uozumi, T.2    Beppu, T.3
  • 57
    • 0024306275 scopus 로고
    • Characterization of the precursor of Serratia marcescens serine protease and COOH-terminal processing of the precursor during its excretion through the outer membrane of Escherichia coli
    • Miyazaki, H., Yanagida, N., Horinouchi, S., and Beppu, T. (1989) Characterization of the precursor of Serratia marcescens serine protease and COOH-terminal processing of the precursor during its excretion through the outer membrane of Escherichia coli. J. Bacteriol. 171, 6566-6572
    • (1989) J. Bacteriol. , vol.171 , pp. 6566-6572
    • Miyazaki, H.1    Yanagida, N.2    Horinouchi, S.3    Beppu, T.4
  • 58
    • 0026846393 scopus 로고
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli. FEMS Microbiol. Lett. 92, 73-78
    • (1992) Escherichia Coli. FEMS Microbiol. Lett. , vol.92 , pp. 73-78
    • Lee, Y.-C.1    Ohta, T.2    Matsuzawa, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.