Interaction of 3-hydroxybenzoate-6-hydroxylase with cibacron blue

Journal of Enzyme Inhibition and Medicinal Chemistry

Volumn 21, Issue 1, 2006, Pages 47-53

  Sumathi, S ^a,c   Dasgupta, Dipak ^b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

^c INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

3 hydroxybenzoate; 3 hydroxybenzoate 6 hydroxylase; Cibacron blue; Circular dichroism; Competitive; Flavin; Fluorescence; Inhibition; Monooxygenase; Uncompetitive

Indexed keywords

3 HYDROXYBENZOIC ACID 6 HYDROXYLASE; AROMATIC AMINO ACID; CIBACRON BLUE F3GA; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; 3 HYDROXYBENZOATE 6 HYDROXYLASE; 3-HYDROXYBENZOATE-6-HYDROXYLASE; CIBACRON BLUE F 3GA; ENZYME INHIBITOR; MIXED FUNCTION OXIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; TRIAZINE DERIVATIVE;

AMINO ACID ANALYSIS; ARTICLE; CHEMICAL ANALYSIS; COMPETITIVE INHIBITION; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; FLUORESCENCE; FLUOROMETRY; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; RESIDUE ANALYSIS; SENSITIVITY ANALYSIS; STOICHIOMETRY; AFFINITY CHROMATOGRAPHY; BINDING SITE; CIRCULAR DICHROISM; DRUG ANTAGONISM; HUMAN; METABOLISM; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

BINDING SITES; CHROMATOGRAPHY, AFFINITY; CIRCULAR DICHROISM; ENZYME INHIBITORS; FLUORESCENCE; HUMANS; MIXED FUNCTION OXYGENASES; NAD; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRIAZINES;

EID: 33646115822     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/02781070500323047     Document Type: Article

References (29)

1. Groseclose, EE and Ribbons, DW. (1973) Biochem Biophys Res Commun, 55, pp. 897-903.
2. Wang, L-H and Hamzah, RY and Yu, Y and Tu, S-C. (1987) Biochemistry, 26, pp. 1099-1104.
3. Yu, Y and Wang, L-H and Tu, S-C. (1987) Biochemistry, 26, pp. 1105-1110.
4. Sumathi, R and Rajasekharan, R and Vaidyanathan, CS. (1990) Arch Biochem Biophys, 278, pp. 21-25.
5. Jones, DCN and Cooper, RA. (1990) Arch Microbiol, 154, pp. 489-495.
6. Suarez, M and Ferrer, E and Garrido-Pertierra, A and Martin, M. (1995) FEMS Microbiol Lett, 126, pp. 283-290.
7. Lineweaver, H and Burk, D. (1934) J Amer Chem Soc, 56, pp. 658-666.
8. Cleland, WW.(1970) The enzymes 3rd ed. New York, USA: Academic press.
9. Dixon, M. (1953) Biochem J, 55, pp. 170-171.
10. Ward, LD. (1985) Meth Enzymol, 117, pp. 400-414.
11. Stinson, RA and Holbrook, JJ. (1973) Biochem J, 131, pp. 719-728.
12. Thompson, ST and Cass, KH and Stellwagen, E. (1975) Proc Natl Acad Sci, 72, pp. 669-672.
13. Thompson, ST and Stellwagen, E. (1976) Proc Natl Acad Sci, 73, pp. 361-365.
14. Stellwagen, E. (1977) Acc Chem Res, 10, pp. 92-98.
15. Stellwagen, E and Baker, B. (1976) Nature, 261, pp. 719-720.
16. Einarsson, R and Eklund, H and Zeppezauer, E and Boiwe, T and Branden, CI. (1974) Eur J Biochem, 49, pp. 41-47.
17. Federici, MM and Chock, PB and Stadtman, ER. (1985) Biochemistry, 24, pp. 647-660.
18. Yang, M and Kirley, TL. (2004) Biochemistry, 43, pp. 9185-9194.
19. He, LZ and Sun, Y. (2002) Bioprocess Biosyst Eng, 25, pp. 155-164.
20. Ryan, LD and Vestling, CS. (1974) Arch Biochem Biophys, 160, pp. 279-284.
21. Watson, DH and Harvey, MJ and Dean, PD. (1978) Biochem J, 173, pp. 591-596.
22. Muller, F and van Berkel, WJH and Steennis, PJ. (1983) Biochem Int, 7, pp. 115-122.
23. Apps, DK and Gleed, CD. (1976) Biochem J, 159, pp. 441-443.
24. Ashton, AR and Polya, GM. (1978) Biochem J, 175, pp. 501-506.
25. Lepo, JE and Stacey, C and Wyss, O and Tabita, FR. (1979) Biochim Biophys Acta, 568, pp. 428-436.
26. Ramesh, KS and Appaji Rao, N. (1980) Biochem J, 187, pp. 249-252.
27. Kapoor, M and O'Brien, MD. (1980) Can J Microbiol, 26, pp. 613-621.
28. Edwards, RA and Woody, RW. (1977) Biochem Biophys Res Commun, 79, pp. 470-476.
29. Edwards, RA and Woody, RW. (1979) Biochemistry, 18, pp. 5197-5204.