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College of Biomedical Science
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Department of Basic Science
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Brew, Keith Dr.
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- B.Sc. (Hons), University College London, Biochemistry, London, U.K.,1962.
- Ph.D., University of London, Courtauld Inst. of Biochemistry, London, U.K., 1966.
- Protein engineering, with an emphasis on regulatory protein-protein interactions and the role of protein dynamics in such interactions.
- Professor, Department of Biochemistry and Molecular Biology, University of Miami, 1977-2001.
- Vice Chairman, Department of Biochemistry and Molecular Biology, University of Miami, 1989-1991.
- Interim CoChair, 1991-95.
- Associate Professor of Biochemistry, University of Miami, 1974-77.
- Lecturer, Department of Biochemistry, University of Leeds, 1968-74.
- Zhang, Y., Deshpande, A., Xie, Z, Natesh, R., Acharya, K.R., and Brew, K. Roles of active site tryptophans in substrate binding and catalysis. by a-1,3 galactosyltransferase. Glycobiology 14, 1295-1302,(2004).
- Azzarolo, A.M., Brew, K., Kota, S., Ponomareva, O., Schwartz, J., and Zylberberg, C. Presence of tear lipocalin and other major proteins in lacrimal fluid of NZW rabbits. Comp. Biochem. Physiol. 138, 111-117, (2004).
- Zhang, Y., Swaminanthan, G.J., Deshpande, A., Natesh, R., Boix, E., Xie, Z., Acharya, K.R., and Brew, K. Roles of individual enzyme-substrate interactions by a-1,3 galactosyltransferase in catalysis and specificity. Biochemistry, in press. (2003).
- Wei, S., Xie, Z., Filenova, E., and Brew, K. Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3. Biochemistry, 42, 12200-12207, (2003).
- Greene, L.H., Hamada, D., Eyles, S.J., and Brew, K. Conserved signature proposed for folding in the lipocalin superfamily. FEBS Lett .553, 39-44. (2003).
- Brew, K. Structure of human ACE gives new insights into inhibitor binding and design. Trends Pharmacol. Sci 24, 391-394, (2003).
- Wei, S., Chen, Y., Chung, L., Nagase, H., and Brew, K. Protein engineering of TIMP-1 inhibitory domain; in search of specific MMP inhibitors. J. Biol. Chem. 278, 9831-9834, (2003).
- Arumugam, S., Gao, G., Patton, B.L., Semechenko, V., Brew, K., and Van Doren, S.R. Increased backbone mobility in b-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. J. Mol. Biol. 373, 719-734, (2003).
- Troeberg, L., Tanaka, M., Wait R., Shi, Y.E., Brew, K., and Nagase, H.E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A). Biochemistry, 41, 15025-15035, (2002).
- Nagase, H., and Brew, K. Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics. Arthritis Research 4 Suppl.3, S51-S61, (2002).
- Boix, E., Zhang, Y., Swaminathan, G.J., Brew, K., and Acharya, K.R.Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase: a-1,3 galactosyltransferase. J. Biol. Chem 277, 28310-28318, (2002).
- Nagase, H., and Brew, K. Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics. Arthritis Research 4 Suppl.3, S51-S61, (2002).
- Zhang, Y., and Brew, K. Alpha-Lactalbumin. In “Encyclopedia of Dairy Sciences” (Ed by Fox, P., and McSweeney, P.) Elsevier Science Ltd., publishers. In press.(2002).
- Boix, E., Swaminathan, G.J., Zhang, Y., Natesh, R., Brew, K. and Acharya, K.R. Structure of UDP complex of UDP-galactose: beta-galactoside-alpha-1,3-galactosyltransferase at 1.53Å resolution reveals a conformational change in the catalytically important C-terminus. Boix, E., Swaminathan, J. Biol. Chem. 276, 48608-48614, (2001).
- Greene, L.H., Chrysina, E.D., Irons, L.I., Papageorgiou, A.C., Acharya, K.R. and Brew, K. Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. Protein Science, 10, 2301-2316, (2001).
- Brew, K., Alpha-Lactalbumin. (Invited Review) In "Advanced Dairy Chemistry-2" (Ed by McSweeney, P.) in press, (2001).
- Kashiwagi, M., Tortorella, M., Nagase, H., and Brew, K.TIMP-3 Is a Potent Inhibitor of ADAM-TS4 (Aggrecanase 1) and ADAM-TS5 (Aggrecanase 2). J. Biol. Chem. 276, 12501-12504 (Accelerated publication), (2001).
- Zhang, Y., Wang, P.G., and Brew, K. Specificity and mechanism of metal ion activation in UDP-galactose beta-galactoside alpha-1,3-galactosyltransferase. J. Biol. Chem. 276, 11567-11574, (2001).
- Brew, K., and Acharya, K.R. Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2.2 Å resolution reveal an effect of Ca2+ on inter-lobe interactions. Chrysina, E.D., J. Biol. Chem. 275, 37021-37029, (2000).
- Nagase, H., Das, S.K., Dey, S.K., Fowlkes, J.L., Huang, W., and Brew, K. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): physiological roles and structural basis of MMP inhibition by TIMP-1. In "Tissue inhibitors of metalloproteinases in development and disease" pp. 3-10. (ed. By Hawkes, S.P., Edwards, D.R., and Khokha, R.) Harwood Academic Publishers, (2000).
- Yu, W-H., Yu, S.C., Meng, Q., Brew, K., and Woessner, F.F.TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix. J. Biol. Chem. 275, 31226-31232, (2000).
- Yu, W-H., Yu, S.C., Meng, Q., Brew. K., and Woessner, F.F.nMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix. submitted to J. Biol. Chem, (2000).
- Brew. K. , Dinakarpandian, D. , and Nagase, H. Tissue Inhibitors of Metalloproteinases (TIMPs): Evolution, Structure and Function. (Invited Review). Biochem. Biophys. Acta, in press, (2000).
- Wu, B., Lee, G., Semenchenki, V ., Huang, W., Brew. K., and Van Doren, S.R. NMR Structure of Tissue Inhibitor of Metalloproteinases-1 Implicates Partial Induced Fit in Recognition of Matrix Metalloproteinases. I. Mol. Biol. 295, 257-268, (2000).
- Wu, B., Huang, W., Brew. K., and Van Doren, S.R. IH, IJC and IsN Resonance Assignments and Secondary Structure of the N- Terminal Domain of Human Tissue Inhibitor of Metalloproteinases-l. I. Biomolecular NMR 3, 14, 289-290, (1999).
- Forge, V ., Wijesinha, R. T., Balbach, I., Brew. K., Robinson, C. V ., Redfield, C., and Dobson, C.M.Rapid Collapse and Slow Structural Reorganization During the Refolding of Bovine a.-Lactalbumin. J. Mol. Biol. 288, 673-688, (1999).
- Greene, L., Grobler, I.A., Malinovskii, V.A., Tian, I., Acharya, K.R., and Brew. K.Stability, Function and Flexibility in a.-Lactalbumin. Protein Engineering, 12, 581-587, (1999).
- Zhang, Y ., Malinovskii, V .A., Fiedler, T, and Brew. K. Role of a Conserved Acidic Cluster in Bovine p 1,4 Galactosyltransferase-1 Probed by Mutagenesis of a Bacterially- Expressed Recombinant Enzyme. Glycobiology, 9, 815-822v (1999).
- Nagase, H., Meng, Q., Malinovskii, V.A., Huang, W., Chung, L., Bode, W., Maskos, K., and Brew. K. Engineering of Selective TIMPs. Ann. N.Y. Acad. Sci., 878, 1-11, (1999).
- Meng, Q., Malinovskii, V.A., Huang, W., Hu, Y., Chung, L., Nagase, H., Bode, W., Maskosa, K., and Brew. K.Residue 2 of Tllv1P-l is a Major Determinant of Affinity and Specificity for Matrix Metalloproteinases but Effects of Substitutions Do Not Correlate with those of Corresponding P1 ' Residue of Substrate. J. Biol. Chem., 274, 10184-10189, (1999).
- Fang, I., Li, I., Chen, X., Zhang, Y., Wang, I., Guo, Z., Zhang, W., Yu, L., Brew. K., and Wang, P.G.Highly Efficient Chemoenzymatic Synthesis of a.-Galactosyl Epitopes with a Recombinant a.(1 ~3)- Galactosyltransferase. J. Am. Chem. Soc. 120, 6635-6638, (1998).
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