Function of interdomain α-helix in human brain hexokinase: Covalent linkage and catalytic regulation between N- and C-terminal halves

Journal of Biomedical Science

Volumn 14, Issue 2, 2007, Pages 195-202

  Tsai, Henry J ^a  

^a DEVELOPMENT CENTER FOR BIOTECHNOLOGY   (Taiwan)

Author keywords

Glucose 6 phosphate inhibition; Inorganic phosphate relief; Interdomain helix; Mammalian hexokinase

Indexed keywords

HEXOKINASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; COVALENT BOND; ENZYME REGULATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; SIGNAL TRANSDUCTION; WILD TYPE;

AMINO ACID SUBSTITUTION; BRAIN; CATALYSIS; HEXOKINASE; HEXOSEPHOSPHATES; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

MAMMALIA;

EID: 34247222009     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1007/s11373-006-9123-5     Document Type: Article

References (25)

1. Grossbard L. and Schimke R.T., Multiple hexokinases of rat tissues. Purification and comparison of soluble forms. J. Biol. Chem. 241(15) 3546-3560, 1966.
2. Wilson J.E., An introduction to the isoenzymes of mammalian hexokinase types I-III. Biochem. Soc. Trans. 25(1) 103-107, 1997.
3. Wilson J.E., Hexokinases. Rev. Physiol. Biochem. Pharmacol. 126: 65-198, 1995.
4. Easterby J.S., The polypeptide chain molecular weight of a mammalian hexokinase. FEBS Lett. 18(1) 23-26, 1971.
5. Colowick S.P., The hexokinases. In: Boyer P.D. (Ed.), The Enzymes. vol. 9, 3rd ed. Academic Press, New York, 1973, pp. 1c-48c.
6. Tsai H.J. and Wilson J.E., Functional organization of mammalian hexokinases: both N- and C-terminal halves of the rat type II isozyme possess catalytic sites. Arch. Biochem. Biophys. 329(1) 17-23, 1996.
7. Ardehali H., Yano Y., Printz R.L., Koch S., Whitesell R.R., May J.M. and Granner D.K., Functional organization of mammalian hexokinase II. Retention of catalytic and regulatory functions in both the NH2- and COOH-terminal halves. J. Biol. Chem. 271(4) 1849-1852, 1996.
8. White T.K. and Wilson J.E., Rat brain hexokinase: location of the allosteric regulatory site in a structural domain at the N-terminus of the enzyme. Arch. Biochem. Biophys. 259(2) 402-411, 1987.
9. White T.K. and Wilson J.E., Isolation and characterization of the discrete N- and C-terminal halves of rat brain hexokinase: retention of full catalytic activity in the isolated C-terminal half. Arch. Biochem. Biophys. 274(2) 375-393, 1989.
10. Tsai H.J. and Wilson J.E., Functional organization of mammalian hexokinases: characterization of the rat type III isozyme and its chimeric forms, constructed with the N-and C-terminal halves of the type I and type II isozymes. Arch. Biochem. Biophys. 338(2) 183-192, 1997.
11. Arora K.K., Filburn C.R. and Pedersen P.L., Structure/function relationships in hexokinase. Site-directed mutational analyses and characterization of overexpressed fragments implicate different functions for the N- and C-terminal halves of the enzyme. J. Biol. Chem. 268(24) 18259-18266, 1993.
12. Tsai H.J., Functional organization and evolution of mammalian hexokinases: mutations that caused the loss of catalytic activity in N-terminal halves of type I and type III isozymes. Arch. Biochem. Biophys. 369(1) 149-156, 1999.
13. Tsai H.J. and Wilson J.E., Functional organization of mammalian hexokinases: characterization of chimeric hexokinases constructed from the N- and C-terminal domains of the rat type I and type II isozymes. Arch. Biochem. Biophys. 316(1) 206-214, 1995.
14. Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J. and Honzatko R.B., Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J. Mol. Biol. 282(2) 345-357, 1998.
15. Liu F., Dong Q., Myers A.M. and Fromm H.J., Expression of human brain hexokinase in Escherichia coli: purification and characterization of the expressed enzyme. Biochem. Biophys. Res. Commun. 177(1) 305-311, 1991.
16. Aleshin A.E., Malfois M., Liu X., Kim C.S., Fromm H.J., Honzatko R.B., Koch M.H. and Svergun D.I., Nonaggregating mutant of recombinant human hexokinase I exhibits wild-type kinetics and rod-like conformations in solution. Biochemistry 38(26) 8359-8366, 1999.
17. Perrella F.W., EZ-FIT: a practical curve-fitting microcomputer program for the analysis of enzyme kinetic data on IBM-PC compatible computers. Anal. Biochem. 174(2) 437-447, 1988.
18. Ferrari R.A., Mandelstam P. and Crane R.K., 1,5-Anhydro-D-glucitol 6-phosphate and its use for the specific inhibition of the hexokinase reaction in tissue homogenates. Arch. Biochem. Biophys. 80(2) 372-377, 1959.
19. Slein M.W., Synthesis of mannose-6-phosphate by hexokinase In: Colowick S. P. and N. O. Kaplan (Eds), Methods Enzymol. vol. 3, Academic Press, New York, 1957, pp. 154-157.
20. Smith R.J. and Caruso J.L., Determination of phosphorus In: Methods Carbohydrate Chem. vol. IV, Academic Press, New York, 1964, pp. 42-46.
21. Sui D. and Wilson J.E., Functional interactions between the noncovalently associated N- and C-terminal halves of mammalian Type I hexokinase. Arch. Biochem. Biophys. 401(1) 21-28, 2002.
22. Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D., Fromm H.J. and Honzatko R.B., Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J. Mol. Biol. 296(4) 1001-1015, 2000.
23. Bright J.N., Shrivastava I.H., Cordes F.S. and Sansom M.S., Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies. Biopolymers 64(6) 303-313, 2002.
24. Hashimoto M. and Wilson J.E., Kinetic and regulatory properties of HK I(+), a modified form of the type I isozyme of mammalian hexokinase in which interactions between the N- and C-terminal halves have been disrupted. Arch. Biochem. Biophys. 399(1) 109-115, 2002.
25. Ardehali H., Printz R.L., Whitesell R.R., May J.M. and Granner D.K., Functional interaction between the N- and C-terminal halves of human hexokinase II. J. Biol. Chem. 274(23) 15986-15989, 1999.