메뉴 건너뛰기




Volumn 48, Issue 9, 2010, Pages 746-750

Soybean (Glycine max) urease: Significance of sulfhydryl groups in urea catalysis

Author keywords

DTNB; IAM; NEM; P CMB; Soybean urease; Sulfhydryl groups

Indexed keywords

GLYCINE MAX;

EID: 77955653591     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2010.05.007     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 0031808511 scopus 로고    scopus 로고
    • The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65 Å resolution
    • Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S. The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65 Å resolution. J. Biol. Inorg. Chem. 1998, 3:268-273.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 268-273
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Ciurli, S.4    Mangani, S.5
  • 2
    • 0033081891 scopus 로고    scopus 로고
    • A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels
    • Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S. A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels. Structure 1999, 7:205-216.
    • (1999) Structure , vol.7 , pp. 205-216
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 4
    • 0036848915 scopus 로고    scopus 로고
    • Purification and characterization of urease from dehusked pigeonpea (Cajanus cajan L.) seeds
    • Das N., Kayastha A.M., Srivastava P.K. Purification and characterization of urease from dehusked pigeonpea (Cajanus cajan L.) seeds. Phytochemistry 2002, 61:513-521.
    • (2002) Phytochemistry , vol.61 , pp. 513-521
    • Das, N.1    Kayastha, A.M.2    Srivastava, P.K.3
  • 5
    • 0019021670 scopus 로고
    • Jack bean urease (EC 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by β-mercaptoethanol, phosphoramidate, and fluoride
    • Dixon N.E., Blakeley R.L., Zerner B. Jack bean urease (EC 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by β-mercaptoethanol, phosphoramidate, and fluoride. Can. J. Biochem. 1980, 58:481-488.
    • (1980) Can. J. Biochem. , vol.58 , pp. 481-488
    • Dixon, N.E.1    Blakeley, R.L.2    Zerner, B.3
  • 6
    • 0034141230 scopus 로고    scopus 로고
    • Purification and properties of urease from leaf of mulberry, Morus alba
    • Hirayama C., Sugimura M., Saito H., Nakamura M. Purification and properties of urease from leaf of mulberry, Morus alba. Phytochemistry 2000, 53:325-330.
    • (2000) Phytochemistry , vol.53 , pp. 325-330
    • Hirayama, C.1    Sugimura, M.2    Saito, H.3    Nakamura, M.4
  • 7
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. The crystal structure of urease from Klebsiella aerogenes. Science 1995, 268:998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 8
    • 9444234584 scopus 로고    scopus 로고
    • Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants
    • Jabri E., Karplus P.A. Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants. Biochemistry 1996, 35:10616-10626.
    • (1996) Biochemistry , vol.35 , pp. 10616-10626
    • Jabri, E.1    Karplus, P.A.2
  • 9
    • 0007825588 scopus 로고
    • An easy method to determine the kinetic parameters of biphasic reactions
    • Kayastha A.M., Gupta A.K. An easy method to determine the kinetic parameters of biphasic reactions. Biochem. Edu. 1987, 15:135-136.
    • (1987) Biochem. Edu. , vol.15 , pp. 135-136
    • Kayastha, A.M.1    Gupta, A.K.2
  • 10
    • 63249111145 scopus 로고    scopus 로고
    • Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: analytical applications
    • Kumar S., Dwevedi A., Kayastha A.M. Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: analytical applications. J. Mol. Catal. B. Enz. 2009, 58:138-145.
    • (2009) J. Mol. Catal. B. Enz. , vol.58 , pp. 138-145
    • Kumar, S.1    Dwevedi, A.2    Kayastha, A.M.3
  • 11
    • 63249110058 scopus 로고    scopus 로고
    • Immobilization of jack bean (Canavalia ensiformis) urease on gelatin and its characterization
    • Kumar S., Kansal A., Kayastha A.M. Immobilization of jack bean (Canavalia ensiformis) urease on gelatin and its characterization. Orien. Pharm. Exp. Med. 2005, 5(1):43-47.
    • (2005) Orien. Pharm. Exp. Med. , vol.5 , Issue.1 , pp. 43-47
    • Kumar, S.1    Kansal, A.2    Kayastha, A.M.3
  • 12
    • 77955663065 scopus 로고    scopus 로고
    • Acetohydroxamic acid: a competitive inhibitor of urease from soybean (Glycine max)
    • Kumar S., Kayastha A.M. Acetohydroxamic acid: a competitive inhibitor of urease from soybean (Glycine max). J. Protein Proteomics 2010, 1:3-8.
    • (2010) J. Protein Proteomics , vol.1 , pp. 3-8
    • Kumar, S.1    Kayastha, A.M.2
  • 13
    • 77955655029 scopus 로고    scopus 로고
    • Inhibition studies of soybean (Glycine max) urease with heavy metals, sodium salts of mineral acids, boric acid and boronic acids
    • doi:10.3109/14756360903468155, in press
    • S. Kumar, A.M. Kayastha, Inhibition studies of soybean (Glycine max) urease with heavy metals, sodium salts of mineral acids, boric acid and boronic acids, J. Enz. Inhib. Med. Chem., in press, doi:10.3109/14756360903468155.
    • J. Enz. Inhib. Med. Chem.
    • Kumar, S.1    Kayastha, A.M.2
  • 15
    • 0007866938 scopus 로고
    • Chemical inactivation and active site groups of phosphoenolpyruvate-phosphatase from germinating mung beans (Vigna radiata)
    • Malhotra O.P., Kayastha A.M. Chemical inactivation and active site groups of phosphoenolpyruvate-phosphatase from germinating mung beans (Vigna radiata). Plant Sci. 1989, 65:161-170.
    • (1989) Plant Sci. , vol.65 , pp. 161-170
    • Malhotra, O.P.1    Kayastha, A.M.2
  • 17
    • 0024514293 scopus 로고
    • Microbial ureases: significance, regulation, and molecular characterization
    • Mobley H.L.T., Hausinger R.P. Microbial ureases: significance, regulation, and molecular characterization. Microbiol. Rev. 1989, 53:85-108.
    • (1989) Microbiol. Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 18
    • 0017123983 scopus 로고
    • A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe
    • Norris G., Brocklehurst K. A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe. Biochem. J. 1976, 159:245-257.
    • (1976) Biochem. J. , vol.159 , pp. 245-257
    • Norris, G.1    Brocklehurst, K.2
  • 19
    • 0018786246 scopus 로고
    • Comparisons of soybean urease isolated from seed and tissue culture
    • Polacco J.C., Havir E.A. Comparisons of soybean urease isolated from seed and tissue culture. J. Biol. Chem. 1979, 254:1707-1715.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1707-1715
    • Polacco, J.C.1    Havir, E.A.2
  • 20
    • 0031957690 scopus 로고    scopus 로고
    • A study of inhibition of urease from seeds of the water melon (Citrullus vu1garis)
    • Prakash O., Bhushan G. A study of inhibition of urease from seeds of the water melon (Citrullus vu1garis). J. Enz. Inhib. Med. Chem. 1998, 13:69-77.
    • (1998) J. Enz. Inhib. Med. Chem. , vol.13 , pp. 69-77
    • Prakash, O.1    Bhushan, G.2
  • 21
    • 0037329922 scopus 로고    scopus 로고
    • Effect of thiols on the activity of urease from dehusked seeds of watermelon (Citrullus vulgaris)
    • Prakash O., Upadhyay L.S.B. Effect of thiols on the activity of urease from dehusked seeds of watermelon (Citrullus vulgaris). Plant Sci. 2003, 164:189-194.
    • (2003) Plant Sci. , vol.164 , pp. 189-194
    • Prakash, O.1    Upadhyay, L.S.B.2
  • 22
    • 0001439739 scopus 로고
    • Determination of thiol and disulphide content: reversible inactivation of the enzyme by the blocking of the unique cysteine residue
    • Riddles P.W., Andrews R.K., Blakeley R.L., Zerner B. Determination of thiol and disulphide content: reversible inactivation of the enzyme by the blocking of the unique cysteine residue. Biochim. Biophys. Acta 1983, 743:115-120.
    • (1983) Biochim. Biophys. Acta , vol.743 , pp. 115-120
    • Riddles, P.W.1    Andrews, R.K.2    Blakeley, R.L.3    Zerner, B.4
  • 23
    • 0034623445 scopus 로고    scopus 로고
    • Significance of sulfhydryl groups in the activity of urease from pigeonpea (Cajanus cajan L.) seeds
    • Srivastava P.K., Kayastha A.M. Significance of sulfhydryl groups in the activity of urease from pigeonpea (Cajanus cajan L.) seeds. Plant Sci. 2000, 159:149-158.
    • (2000) Plant Sci. , vol.159 , pp. 149-158
    • Srivastava, P.K.1    Kayastha, A.M.2
  • 24
    • 0000997583 scopus 로고
    • Academic Press Inc., New York, J.B. Sumner, K. Myrbark (Eds.)
    • Sumner J.B. The Enzyme 1951, 873-879. Academic Press Inc., New York. J.B. Sumner, K. Myrbark (Eds.).
    • (1951) The Enzyme , pp. 873-879
    • Sumner, J.B.1
  • 25
    • 35048849832 scopus 로고    scopus 로고
    • Immobilization of urease from pigeonpea (Cajanas cajan) on agar tablets and its application in urea assay
    • Swati M., Kumar S., Reddy K.R.S., Kayastha A.M. Immobilization of urease from pigeonpea (Cajanas cajan) on agar tablets and its application in urea assay. Appl. Biochem. Biotechnol. 2007, 142:291-297.
    • (2007) Appl. Biochem. Biotechnol. , vol.142 , pp. 291-297
    • Swati, M.1    Kumar, S.2    Reddy, K.R.S.3    Kayastha, A.M.4
  • 26
    • 0023481419 scopus 로고
    • Location of the essential cysteine residue of jack bean urease
    • Takishima K., Mamiya G. Location of the essential cysteine residue of jack bean urease. Protein Seq. Data Anal. 1987, 1:103-106.
    • (1987) Protein Seq. Data Anal. , vol.1 , pp. 103-106
    • Takishima, K.1    Mamiya, G.2
  • 27
    • 0024288267 scopus 로고
    • The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues
    • Takishima K., Suga T., Mamiya G. The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues. Eur. J. Biochem. 1988, 175:151-165.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 151-165
    • Takishima, K.1    Suga, T.2    Mamiya, G.3
  • 28
    • 0026355724 scopus 로고
    • Identification of the essential cysteine residue in Klebsiella aerogenes urease
    • Todd M.J., Hausinger R.P. Identification of the essential cysteine residue in Klebsiella aerogenes urease. J. Biol. Chem. 1991, 266:24327-24331.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24327-24331
    • Todd, M.J.1    Hausinger, R.P.2
  • 29
    • 0025744894 scopus 로고
    • Reactivity of the essential thiol of Klebsiella aerogenes urease. Effect of pH and ligands on thiol modification
    • Todd M.J., Hausinger R.P. Reactivity of the essential thiol of Klebsiella aerogenes urease. Effect of pH and ligands on thiol modification. J. Biol. Chem. 1991, 266:10260-10267.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10260-10267
    • Todd, M.J.1    Hausinger, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.