Chemical modification of catalytic site of lipase from wheat germ: Altered structure-activity profile

Indian Journal of Biochemistry and Biophysics

Volumn 39, Issue 1, 2002, Pages 28-34

  Gopalakrishna, K N ^a   Ramesh Kumar, P ^a   Prakash, V ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; ASPARAGINE; BENZYLSULFONYL FLUORIDE; CARBOXYL GROUP; DIETHYL PYROCARBONATE; GLUTAMINE; HISTIDINE; SERINE; TRIACYLGLYCEROL LIPASE;

ARTICLE; CALORIMETRY; CATALYSIS; CATALYST; CHEMICAL MODIFICATION; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MODIFICATION; FLUORESCENCE SPECTROSCOPY; MICROENVIRONMENT; NONHUMAN; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY; WHEAT GERM;

ASPARTIC ACID; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYTIC DOMAIN; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; HISTIDINE; HOT TEMPERATURE; KINETICS; LIPASE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SERINE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; TRITICUM;

TRITICUM AESTIVUM;

EID: 0042766509     PISSN: 03011208     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Imoto T & Yamada H (1997) in Protein Function: A Practical Approach (Creighton T E, ed), pp. 279-316, IRL Press, New York
2. Glazer A N, DeLange R J & Sigman D S (1976) in Chemical Modifications of Proteins (Work T S & Work E, eds), Laboratory Techniques in Biochemistry and Molecular Biology Vol 4, Part I, North Holland Publishing Company, Amsterdam
3. Colman R F (1989) in Protein Function: A Practical Approach (Creighton T E, ed) IRL Press, Oxford
4. Brady L, Brzozowski A M, Derewenda Z S, Dodson E, Dodson G, Tolley S, Turkenberg J P, Christiansen L, Huge-Jensen B, Norskov L, Thim L & Menge U (1990) Nature (London) 343, 767-770
5. Schrag J D, Li Y, Wu S & Cygler M (1991) Nature (London) 351, 761-764
6. Winkler F K, D'Acry A & Hunziker W (1990) Nature (London) 343, 771-774
7. Rajeshwara A N & Prakash V (1994) Int J Peptide Protein Res 44, 435-440
8. th edn,. pp. 988, Association of Official Analytical Chemist's Inc. Virginia, USA
9. Sudhindra Rao K, Rajendran S, Rajeshwara A N & Prakash V (1991) J Protein Chem 10, 291-299
10. Takagi S, Kobayashi M & Matsuda K (1989) J Biochem (Tokyo) 105, 933-938
11. Chen Y H & Yang J T (1971) Biochem Biophys Res Commun 44, 1285-1291
12. Arakawa T, Bhat R & Timasheff S N (1990) Biochemistry 29, 1924-1931
13. Meyer S E & Cromartie T H (1980) Biochemistry 19, 1874-1881
14. Wakayama M, Tsutsumi T, Yada H, Sakai K & Moriguchi M (1996) Biosci Biotech Biochem 60, 650-653
15. Rajeshwara A N (1994) Physico-chemical Properties of Plant Lipases, Ph D thesis, University of Mysore, Mysore, India
16. Miles E W (1977) Methods Enzymol 47, 431-442
17. Muhlrad A, Hegyi G & Toth G (1967) Acta Biochim Biophys Acad Sci Hung 19, 19-29
18. Garrison K C & Himes R H (1975) Biochem Biophys Res Commun 67, 1251-1255
19. Melchoir Jr W B & Fahrney D (1970) Biochemistry 9, 251-258
20. Riehm & Scheraga H A (1996) Biochemistry 5, 99-115
21. Ariki M & Fukui T (1978) J Biochem (Tokyo) 83, 183-190
22. Iwama M, Ohtsuki R, Takahashi T & Irie M (1984) J Biochem (Tokyo) 96, 329-336
23. Subray S H, Ameeta R K, Krishna W G & Khan I M (1998) Arch Biochem Biophys 355, 153-159
24. Okada M, Kawashima S & Imahori K (1980) J Biochem 88, 481-488
25. Grochulski P, Bouthillier F, Kazlauskas R J, Serreqi A N, Schrag J D, Ziomek E & Cygler M (1994) Biochemistry 33, 3494-3500